{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T04:52:49Z","timestamp":1791089569212,"version":"4.1.0"},"reference-count":153,"publisher":"MDPI AG","issue":"19","license":[{"start":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T00:00:00Z","timestamp":1790899200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Yuelushan Laboratory Project","award":["YLS-2025-ZY01008"],"award-info":[{"award-number":["YLS-2025-ZY01008"]}]},{"name":"Hunan Provincial Science and Technology Talent Lift Project","award":["2023TJ-Z09"],"award-info":[{"award-number":["2023TJ-Z09"]}]},{"name":"Science and Technology Innovation Program of Hunan Province","award":["2023RC1077"],"award-info":[{"award-number":["2023RC1077"]}]},{"name":"Natural Science Foundation of Hunan Province","award":["2023JJ20311"],"award-info":[{"award-number":["2023JJ20311"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biology"],"abstract":"<jats:p>This review presents a three-tiered engineering framework that systematically addresses these barriers. First, we survey chemical and sequence-based stabilization strategies, including lipidation, backbone N-methylation, and cyclization, that convert labile natural peptides into protease-resistant scaffolds. Second, moving beyond generic stabilization, we dissect the rational design of effector-inhibitory peptides, with particular emphasis on disulfide bond topology engineering as a powerful means to lock binding-competent conformations, alongside structure-guided interface optimization. Third, recognizing that purely rational design often fails to correctly fold complex topologies, we discuss complementary structure-constrained screening platforms (phage display, yeast display, and in silico docking) that exploit sequence\u2013conformation coupling to enrich functional structures from vast libraries. Critically, we argue that these molecular-level designs can only achieve in vivo efficacy when co-integrated with delivery systems, including lipidic, polymeric, and viral carriers, which together determine bioavailability, targeting, and controlled release. By weaving these layers into a unified framework, we highlight a paradigm shift from sequential optimization toward context-aware co-design, where peptide rigidity, flexibility, affinity, and carrier compatibility are balanced against specific therapeutic or industrial contexts.<\/jats:p>","DOI":"10.3390\/biology15191754","type":"journal-article","created":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T10:14:56Z","timestamp":1790936096000},"page":"1754","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Rational Design and Delivery of Engineered Peptides: Toward a Unified Framework for Structure, Screening, and Application"],"prefix":"10.3390","volume":"15","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-6168-8994","authenticated-orcid":false,"given":"Qijun","family":"Xie","sequence":"first","affiliation":[{"name":"School of Biological Science and Medical Engineering, Hunan University of Technology, Zhuzhou 412007, China"},{"name":"Yuelushan Laboratory, Hunan Academy of Agricultural Sciences, Changsha 410125, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Haiying","family":"Ma","sequence":"additional","affiliation":[{"name":"School of Biological Science and Medical Engineering, Hunan University of Technology, Zhuzhou 412007, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Biao","family":"Liu","sequence":"additional","affiliation":[{"name":"School of Biological Science and Medical Engineering, Hunan University of Technology, Zhuzhou 412007, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Li","family":"Yu","sequence":"additional","affiliation":[{"name":"School of Biological Science and Medical Engineering, Hunan University of Technology, Zhuzhou 412007, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0006-7536-7546","authenticated-orcid":false,"given":"Yang","family":"Fang","sequence":"additional","affiliation":[{"name":"School of Biological Science and Medical Engineering, Hunan University of Technology, Zhuzhou 412007, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lili","family":"Liu","sequence":"additional","affiliation":[{"name":"Hunan Key Laboratory of Economic Crops Genetic Improvement and Integrated Utilization, School of Life and Health Sciences, Hunan University of Science and Technology, Xiangtan 411201, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1725-0682","authenticated-orcid":false,"given":"Mingli","family":"Yan","sequence":"additional","affiliation":[{"name":"Yuelushan Laboratory, Hunan Academy of Agricultural Sciences, Changsha 410125, China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,10,2]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"e2300171","DOI":"10.1002\/mabi.202300171","article-title":"Peptide-Based Optical\/Electronic Materials: Assembly and Recent Applications in Biomedicine, Sensing, and Energy Storage","volume":"23","author":"Tian","year":"2023","journal-title":"Macromol. Biosci."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"963","DOI":"10.1080\/07388551.2023.2254932","article-title":"Pulmonary delivery systems for antimicrobial peptides","volume":"44","author":"Caselli","year":"2024","journal-title":"Crit. Rev. Biotechnol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/S0065-2660(09)67002-4","article-title":"Adeno-associated viral vectors and their redirection to cell-type specific receptors","volume":"67","author":"Michelfelder","year":"2009","journal-title":"Adv. Genet."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"113896","DOI":"10.1016\/j.jconrel.2025.113896","article-title":"Polymer-based coating of adeno-associated viral particles as a new strategy to evade immune response for DMD treatment","volume":"384","author":"Pinto","year":"2025","journal-title":"J. Control. Release"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"855","DOI":"10.1007\/s40262-013-0079-0","article-title":"Pharmacokinetics and pharmacokinetic-pharmacodynamic correlations of therapeutic peptides","volume":"52","author":"Diao","year":"2013","journal-title":"Clin. Pharmacokinet."},{"key":"ref_6","doi-asserted-by":"crossref","unstructured":"Nugrahadi, P.P., Hinrichs, W.L.J., Frijlink, H.W., Sch\u00f6neich, C., and Avanti, C. (2023). Designing Formulation Strategies for Enhanced Stability of Therapeutic Peptides in Aqueous Solutions: A Review. Pharmaceutics, 15.","DOI":"10.3390\/pharmaceutics15030935"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"815","DOI":"10.1016\/j.jcis.2020.08.045","article-title":"Internal liquid crystal structures in nanocarriers containing drug hydrophobic ion pairs dictate drug release","volume":"582","author":"Ristroph","year":"2021","journal-title":"J. Colloid Interface Sci."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"10914","DOI":"10.1039\/D3SC01089A","article-title":"Engineering of antimicrobial peptide fibrils with feedback degradation of bacterial-secreted enzymes","volume":"14","author":"Wang","year":"2023","journal-title":"Chem. Sci."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"123424","DOI":"10.1016\/j.carbpol.2025.123424","article-title":"A sustained H2S-releasing nanocellulose-based hydrogel with anti-inflammatory and antibacterial properties for promoting infected wound healing","volume":"355","author":"Zhao","year":"2025","journal-title":"Carbohydr. Polym."},{"key":"ref_10","doi-asserted-by":"crossref","unstructured":"Recktenwald, M., Kaur, M., Benmassaoud, M.M., Copling, A., Khanna, T., Curry, M., Cortes, D., Fleischer, G., Carabetta, V.J., and Vega, S.L. (2024). Antimicrobial Peptide Screening for Designing Custom Bactericidal Hydrogels. Pharmaceutics, 16.","DOI":"10.3390\/pharmaceutics16070860"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"127231","DOI":"10.1016\/j.ijbiomac.2023.127231","article-title":"Physicochemical, antibacterial and food preservation properties of active packaging films based on chitosan\/\u03b5-polylysine-grafted bacterial cellulose","volume":"253","author":"Liao","year":"2023","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"46493","DOI":"10.1002\/app.46493","article-title":"Effects of hydrophilic\/hydrophobic surfaces on polymer-complexation kinetics","volume":"135","author":"Sayama","year":"2018","journal-title":"J. Appl. Polym. Sci."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1007\/s11010-018-3386-9","article-title":"Biofunctionalized self-assembly of peptide amphiphile induces the differentiation of bone marrow mesenchymal stem cells into neural cells","volume":"450","author":"Ruan","year":"2019","journal-title":"Mol. Cell. Biochem."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"1696","DOI":"10.1016\/S0140-6736(06)69705-5","article-title":"The incretin system: Glucagon-like peptide-1 receptor agonists and dipeptidyl peptidase-4 inhibitors in type 2 diabetes","volume":"368","author":"Drucker","year":"2006","journal-title":"Lancet"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1016\/j.pharmthera.2012.05.009","article-title":"Targeting the glucagon receptor family for diabetes and obesity therapy","volume":"135","author":"Cho","year":"2012","journal-title":"Pharmacol. Ther."},{"key":"ref_16","doi-asserted-by":"crossref","unstructured":"Mahlapuu, M., H\u00e5kansson, J., Ringstad, L., and Bj\u00f6rn, C. (2016). Antimicrobial Peptides: An Emerging Category of Therapeutic Agents. Front. Cell. Infect. Microbiol., 6.","DOI":"10.3389\/fcimb.2016.00194"},{"key":"ref_17","first-page":"3919","article-title":"The antimicrobial peptides and their potential clinical applications","volume":"11","author":"Lei","year":"2019","journal-title":"Am. J. Transl. Res."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"406","DOI":"10.1016\/j.tips.2017.01.003","article-title":"Cell-Penetrating Peptides: From Basic Research to Clinics","volume":"38","author":"Guidotti","year":"2017","journal-title":"Trends Pharmacol. Sci."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"3029","DOI":"10.2174\/0929867043363884","article-title":"Ziconotide: Neuronal calcium channel blocker for treating severe chronic pain","volume":"11","author":"Miljanich","year":"2004","journal-title":"Curr. Med. Chem."},{"key":"ref_20","doi-asserted-by":"crossref","unstructured":"Tyler, T.J., Durek, T., and Craik, D.J. (2023). Native and Engineered Cyclic Disulfide-Rich Peptides as Drug Leads. Molecules, 28.","DOI":"10.3390\/molecules28073189"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"4167","DOI":"10.1021\/jacs.8b13178","article-title":"Macrocyclic Peptides as Drug Candidates: Recent Progress and Remaining Challenges","volume":"141","author":"Vinogradov","year":"2019","journal-title":"J. Am. Chem. Soc."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"746","DOI":"10.1021\/acschembio.4c00878","article-title":"Rational Design of Stapled Covalent Peptide Modifiers of Oncoprotein E6 from Human Papillomavirus","volume":"20","author":"Emanuelson","year":"2025","journal-title":"ACS Chem. Biol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/0142-9612(84)90062-0","article-title":"Controlled biodegradability of polymers\u2014A key to drug delivery systems","volume":"5","author":"Kopecek","year":"1984","journal-title":"Biomaterials"},{"key":"ref_24","doi-asserted-by":"crossref","unstructured":"Dalgicdir, C., Globisch, C., Peter, C., and Sayar, M. (2015). Tipping the Scale from Disorder to Alpha-helix: Folding of Amphiphilic Peptides in the Presence of Macroscopic and Molecular Interfaces. PLoS Comput. Biol., 11.","DOI":"10.1371\/journal.pcbi.1004328"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"107962","DOI":"10.1016\/j.biotechadv.2022.107962","article-title":"Strategies employed in the design of antimicrobial peptides with enhanced proteolytic stability","volume":"59","author":"Lai","year":"2022","journal-title":"Biotechnol. Adv."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"e202425456","DOI":"10.1002\/anie.202425456","article-title":"Intrinsically Disordered Peptide Nanofibers from a Structured Motif Within Proteins","volume":"64","author":"Qiao","year":"2025","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"254","DOI":"10.1002\/anie.201205674","article-title":"N-methylation of peptides and proteins: An important element for modulating biological functions","volume":"52","author":"Chatterjee","year":"2013","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"6008","DOI":"10.1038\/srep06008","article-title":"Serum stable natural peptides designed by mRNA display","volume":"4","author":"Howell","year":"2014","journal-title":"Sci. Rep."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"5910","DOI":"10.1073\/pnas.1605363113","article-title":"Enhancing protein stability with extended disulfide bonds","volume":"113","author":"Liu","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"105353","DOI":"10.1016\/j.jbc.2023.105353","article-title":"Identification of the functional PD-L1 interface region responsible for PD-1 binding and initiation of PD-1 signaling","volume":"299","author":"Carter","year":"2023","journal-title":"J. Biol. Chem."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"4487","DOI":"10.1038\/s41467-025-59665-7","article-title":"Prolonging parathyroid hormone analog action in vitro and in vivo through peptide lipidation","volume":"16","author":"Noda","year":"2025","journal-title":"Nat. Commun."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"2019","DOI":"10.1021\/acs.biochem.5c00826","article-title":"Advanced Peptide Modifications for Superior Therapeutics","volume":"65","author":"Bhadra","year":"2026","journal-title":"Biochemistry"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1602","DOI":"10.2174\/092986712799945003","article-title":"Converting peptides into drug leads by lipidation","volume":"19","author":"Zhang","year":"2012","journal-title":"Curr. Med. Chem."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1269","DOI":"10.1111\/febs.70298","article-title":"Artificial lipidation of proteins and peptides: From mechanism to clinical applications","volume":"293","author":"Mu","year":"2026","journal-title":"FEBS J."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"1942","DOI":"10.1021\/acs.jmedchem.5c02390","article-title":"Fatty Acid-Conjugated Antimicrobial Peptides: Advances in Design, Activity, and Therapeutic Potential","volume":"69","author":"Helmy","year":"2026","journal-title":"J. Med. Chem."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"4916","DOI":"10.1021\/acsbiomaterials.4c00736","article-title":"Quantifying and Controlling the Proteolytic Degradation of Cell Adhesion Peptides","volume":"10","author":"Rozans","year":"2024","journal-title":"ACS Biomater. Sci. Eng."},{"key":"ref_37","doi-asserted-by":"crossref","unstructured":"Lester, C., Li, J.M., Passang, T., Wang, Y., Waller, E.K., and Blakey, S.B. (2024). Chemical Modifications to Enhance the Drug Properties of a VIP Receptor Antagonist (ANT) Peptide. Int. J. Mol. Sci., 25.","DOI":"10.3390\/ijms25084391"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"1331","DOI":"10.1021\/ar8000603","article-title":"N-methylation of peptides: A new perspective in medicinal chemistry","volume":"41","author":"Chatterjee","year":"2008","journal-title":"Acc. Chem. Res."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"2595","DOI":"10.1002\/anie.200705797","article-title":"Improving oral bioavailability of peptides by multiple N-methylation: Somatostatin analogues","volume":"47","author":"Biron","year":"2008","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"891","DOI":"10.1021\/jacs.0c10696","article-title":"Targeting the APP-Mint2 Protein-Protein Interaction with a Peptide-Based Inhibitor Reduces Amyloid-\u03b2 Formation","volume":"143","author":"Bartling","year":"2021","journal-title":"J. Am. Chem. Soc."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"11831","DOI":"10.1021\/acs.jmedchem.3c00406","article-title":"Structure-Activity Relationships of the Antimicrobial Peptide Natural Product Apidaecin","volume":"66","author":"Skowron","year":"2023","journal-title":"J. Med. Chem."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"105453","DOI":"10.1016\/j.ejps.2020.105453","article-title":"Effect of N-methylated and fatty acid conjugation on analogs of antimicrobial peptide Anoplin","volume":"152","author":"Liu","year":"2020","journal-title":"Eur. J. Pharm. Sci."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"14973","DOI":"10.1002\/anie.201708927","article-title":"Conotoxin \u03a6-MiXXVIIA from the Superfamily G2 Employs a Novel Cysteine Framework that Mimics Granulin and Displays Anti-Apoptotic Activity","volume":"56","author":"Jin","year":"2017","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"ref_44","doi-asserted-by":"crossref","unstructured":"Pei, Z., Song, Q., Xu, J., Yu, S., and Ma, H. (2025). The Cyclic Antimicrobial Peptide C-LR18 Has Enhanced Antibacterial Activity, Improved Stability, and a Longer Half-Life Compared to the Original Peptide. Antibiotics, 14.","DOI":"10.3390\/antibiotics14030312"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1038\/s41573-020-00135-8","article-title":"Trends in peptide drug discovery","volume":"20","author":"Muttenthaler","year":"2021","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"6275","DOI":"10.1021\/jm4011675","article-title":"Hydrocarbon-stapled peptides: Principles, practice, and progress","volume":"57","author":"Walensky","year":"2014","journal-title":"J. Med. Chem."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1016\/j.csbj.2019.01.012","article-title":"Stapled Peptides Inhibitors: A New Window for Target Drug Discovery","volume":"17","author":"Ali","year":"2019","journal-title":"Comput. Struct. Biotechnol. J."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"816","DOI":"10.1021\/jacsau.3c00795","article-title":"Development of a Double-Stapled Peptide Stabilizing Both \u03b1-Helix and \u03b2-Sheet Structures for Degrading Transcription Factor AR-V7","volume":"4","author":"Ma","year":"2024","journal-title":"JACS Au"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"117568","DOI":"10.1016\/j.ejmech.2025.117568","article-title":"Design, synthesis, and antitumor activity of stapled peptide inhibitors targeting the RAS-RAF interactions","volume":"290","author":"Han","year":"2025","journal-title":"Eur. J. Med. Chem."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"1643","DOI":"10.1002\/cbic.201600253","article-title":"Directed Evolution of Scanning Unnatural-Protease-Resistant (SUPR) Peptides for in Vivo Applications","volume":"17","author":"Fiacco","year":"2016","journal-title":"Chembiochem"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"9055","DOI":"10.1039\/D1CS00160D","article-title":"Directing evolution of novel ligands by mRNA display","volume":"50","author":"Kamalinia","year":"2021","journal-title":"Chem. Soc. Rev."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"779","DOI":"10.1038\/nprot.2011.331","article-title":"Flexizymes for genetic code reprogramming","volume":"6","author":"Goto","year":"2011","journal-title":"Nat. Protoc."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"1742","DOI":"10.1021\/acs.molpharmaceut.6b01174","article-title":"Highly Selective Targeting of Hepatic Stellate Cells for Liver Fibrosis Treatment Using a d-Enantiomeric Peptide Ligand of Fn14 Identified by Mirror-Image mRNA Display","volume":"14","author":"Huang","year":"2017","journal-title":"Mol. Pharm."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"3604","DOI":"10.1021\/acs.accounts.1c00391","article-title":"The RaPID Platform for the Discovery of Pseudo-Natural Macrocyclic Peptides","volume":"54","author":"Goto","year":"2021","journal-title":"Acc. Chem. Res."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"5680","DOI":"10.1021\/jacs.1c02593","article-title":"In Vitro Selection of Macrocyclic d\/L-Hybrid Peptides against Human EGFR","volume":"143","author":"Imanishi","year":"2021","journal-title":"J. Am. Chem. Soc."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"e202406414","DOI":"10.1002\/anie.202406414","article-title":"mRNA Display in Cell Lysates Enables Identification of Cyclic Peptides Targeting the BRD3 Extraterminal Domain","volume":"63","author":"Hurd","year":"2024","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1039\/D4CB00229F","article-title":"Rational engineering of an antimalarial peptide with enhanced proteolytic stability and preserved parasite invasion inhibitory activity","volume":"6","author":"Kar","year":"2025","journal-title":"RSC Chem. Biol."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"12100","DOI":"10.1021\/acs.jmedchem.0c01500","article-title":"Automated Design of Macrocycles for Therapeutic Applications: From Small Molecules to Peptides and Proteins","volume":"63","author":"Sindhikara","year":"2020","journal-title":"J. Med. Chem."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"7438","DOI":"10.1021\/acs.jmedchem.2c00123","article-title":"Peptidomimetics: An Overview of Recent Medicinal Chemistry Efforts toward the Discovery of Novel Small Molecule Inhibitors","volume":"65","year":"2022","journal-title":"J. Med. Chem."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"592","DOI":"10.1097\/01.mjt.0000178766.60234.e2","article-title":"Peptide-mediated immunosuppression","volume":"12","author":"Zang","year":"2005","journal-title":"Am. J. Ther."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1016\/j.coviro.2011.10.008","article-title":"Interferon-stimulated genes and their antiviral effector functions","volume":"1","author":"Schoggins","year":"2011","journal-title":"Curr. Opin. Virol."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"8982","DOI":"10.1021\/acs.jmedchem.7b01221","article-title":"Structure-Based Design of Non-natural Macrocyclic Peptides That Inhibit Protein-Protein Interactions","volume":"60","author":"Glas","year":"2017","journal-title":"J. Med. Chem."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"17287","DOI":"10.1021\/acs.jmedchem.1c01334","article-title":"Targeting a Novel KRAS Binding Site: Application of One-Component Stapling of Small (5-6-mer) Peptides","volume":"64","author":"Fumagalli","year":"2021","journal-title":"J. Med. Chem."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"1604","DOI":"10.1021\/acschembio.0c00204","article-title":"Covalent Targeting of Ras G12C by Rationally Designed Peptidomimetics","volume":"15","author":"Yoo","year":"2020","journal-title":"ACS Chem. Biol."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1021\/acs.jpcb.3c06678","article-title":"Topological Reaction Coordinate Captures the Folding Transition State Ensemble in a Pierced Lasso Protein","volume":"128","author":"Noel","year":"2024","journal-title":"J. Phys. Chem. B"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"20281","DOI":"10.1073\/pnas.1011686107","article-title":"Structure-based development of a receptor activator of nuclear factor-kappaB ligand (RANKL) inhibitor peptide and molecular basis for osteopetrosis","volume":"107","author":"Ta","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1002\/(SICI)1097-0134(20000701)40:1<168::AID-PROT180>3.0.CO;2-N","article-title":"Disulfide bond plasticity in epidermal growth factor","volume":"40","author":"Komives","year":"2000","journal-title":"Proteins"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"1864","DOI":"10.1099\/mic.0.000569","article-title":"Aeropyrum pernix membrane topology of protein VKOR promotes protein disulfide bond formation in two subcellular compartments","volume":"163","author":"Hibender","year":"2017","journal-title":"Microbiology"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"107525","DOI":"10.1016\/j.pharmthera.2020.107525","article-title":"Role of the ERO1-PDI interaction in oxidative protein folding and disease","volume":"210","author":"Shergalis","year":"2020","journal-title":"Pharmacol. Ther."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"e202504640","DOI":"10.1002\/anie.202504640","article-title":"Antiparallel \u03b2-Sheet as a Key Motif of Amyloid-\u03b2 Inhibitor Designed via Topological Peptide Reprogramming","volume":"64","author":"Im","year":"2025","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"1480","DOI":"10.1021\/acschembio.3c00268","article-title":"Folding-Assisted Peptide Disulfide Formation and Dimerization","volume":"18","author":"Victorio","year":"2023","journal-title":"ACS Chem. Biol."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"969","DOI":"10.1021\/acschembio.2c00114","article-title":"Directed Evolution-Driven Increase of Structural Plasticity Is a Prerequisite for Binding the Complement Lectin Pathway Blocking MASP-Inhibitor Peptides","volume":"17","author":"Boros","year":"2022","journal-title":"ACS Chem. Biol."},{"key":"ref_73","doi-asserted-by":"crossref","unstructured":"Trent, T., Miller, J.J., and Bowman, G.R. (2024). The G protein inhibitor YM-254890 is an allosteric glue. bioRxiv.","DOI":"10.1101\/2024.11.25.625299"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1111\/j.1472-8206.1998.tb00932.x","article-title":"Drugs interacting with G protein alpha subunits: Selectivity and perspectives","volume":"12","author":"Chahdi","year":"1998","journal-title":"Fundam. Clin. Pharmacol."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"115161","DOI":"10.1016\/j.biopha.2023.115161","article-title":"BTLA-derived peptides as inhibitors of BTLA\/HVEM complex formation-design, synthesis and biological evaluation","volume":"165","author":"Kuncewicz","year":"2023","journal-title":"Biomed. Pharmacother."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"23270","DOI":"10.1039\/D1RA03118J","article-title":"Rational design of a potent macrocyclic peptide inhibitor targeting the PD-1\/PD-L1 protein-protein interaction","volume":"11","author":"Miao","year":"2021","journal-title":"RSC Adv."},{"key":"ref_77","doi-asserted-by":"crossref","unstructured":"Peng, W., Gu, W., Chen, W., Zhao, J., Che Ajuyo, N.M., Pei, Y., Min, Y., and Wang, D. (2025). Structure-Guided Design of Cyclic Peptide: A Potent Inhibitor Targeting PD-1\/PD-L1 Axis with Antitumor Activity. Int. J. Mol. Sci., 26.","DOI":"10.3390\/ijms262311308"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"2316","DOI":"10.1016\/j.bmcl.2019.06.022","article-title":"Structure-based design of potent linear peptide inhibitors of the YAP-TEAD protein-protein interaction derived from the YAP omega-loop sequence","volume":"29","author":"Furet","year":"2019","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"15810","DOI":"10.1038\/s41598-022-19703-6","article-title":"Peptidomimetics designed to bind to RAS effector domain are promising cancer therapeutic compounds","volume":"12","author":"Pallara","year":"2022","journal-title":"Sci. Rep."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"10079","DOI":"10.1021\/acs.chemrev.0c00532","article-title":"Stapled Helical Peptides Bearing Different Anchoring Residues","volume":"120","author":"Li","year":"2020","journal-title":"Chem. Rev."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"2547","DOI":"10.1039\/C6SC05710A","article-title":"Artificial disulfide-rich peptide scaffolds with precisely defined disulfide patterns and a minimized number of isomers","volume":"8","author":"Zheng","year":"2017","journal-title":"Chem. Sci."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"16285","DOI":"10.1021\/jacs.0c06044","article-title":"Directed Disulfide Pairing and Folding of Peptides for the De Novo Development of Multicyclic Peptide Libraries","volume":"142","author":"Lu","year":"2020","journal-title":"J. Am. Chem. Soc."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"7461","DOI":"10.1021\/jacs.4c15843","article-title":"Identification of Covalent Cyclic Peptide Inhibitors Targeting Protein-Protein Interactions Using Phage Display","volume":"147","author":"Wang","year":"2025","journal-title":"J. Am. Chem. Soc."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"11847","DOI":"10.1039\/D4SC03207A","article-title":"A facile strategy for the construction of a phage display cyclic peptide library for the selection of functional macrocycles","volume":"15","author":"Xiang","year":"2024","journal-title":"Chem. Sci."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"7143","DOI":"10.1021\/bi0481592","article-title":"New binding specificities derived from Min-23, a small cystine-stabilized peptidic scaffold","volume":"44","author":"Souriau","year":"2005","journal-title":"Biochemistry"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"2128","DOI":"10.1021\/acschembio.6c00501","article-title":"pH-Controlled Stepwise Cyclization Enables Phage Display of Heterobridged Bicyclic Peptide Libraries","volume":"21","author":"Ye","year":"2026","journal-title":"ACS Chem. Biol."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"7308","DOI":"10.1038\/s41467-024-51610-4","article-title":"Proximity-driven site-specific cyclization of phage-displayed peptides","volume":"15","author":"Brown","year":"2024","journal-title":"Nat. Commun."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1016\/j.jmb.2011.10.021","article-title":"The scope of phage display for membrane proteins","volume":"414","author":"Vithayathil","year":"2011","journal-title":"J. Mol. Biol."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1007\/s00253-005-0270-9","article-title":"Phage display systems and their applications","volume":"70","author":"Paschke","year":"2006","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"548","DOI":"10.1021\/bc200613e","article-title":"Fibrin specific peptides derived by phage display: Characterization of peptides and conjugates for imaging","volume":"23","author":"Kolodziej","year":"2012","journal-title":"Bioconjug. Chem."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1007\/978-1-0716-2285-8_9","article-title":"Affinity and Stability Analysis of Yeast Displayed Proteins","volume":"2491","author":"Zajc","year":"2022","journal-title":"Methods Mol. Biol."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"108422","DOI":"10.1016\/j.biotechadv.2024.108422","article-title":"Yeast surface display technology: Mechanisms, applications, and perspectives","volume":"76","author":"Li","year":"2024","journal-title":"Biotechnol. Adv."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1080\/07388551.2024.2385996","article-title":"Strategic approaches for designing yeast strains as protein secretion and display platforms","volume":"45","author":"Xu","year":"2025","journal-title":"Crit. Rev. Biotechnol."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"102913","DOI":"10.1016\/j.jbc.2023.102913","article-title":"Yeast display platform with expression of linear peptide epitopes for high-throughput assessment of peptide-MHC-II binding","volume":"299","author":"Huisman","year":"2023","journal-title":"J. Biol. Chem."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"7689","DOI":"10.1021\/acs.jmedchem.5c02876","article-title":"Yeast Display Technology Enables Rapid Discovery of Low-Nanomolar Macrocyclic Peptide Inhibitors of Human Angiotensin-Converting Enzyme 2","volume":"69","author":"Romanyuk","year":"2026","journal-title":"J. Med. Chem."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"1101","DOI":"10.2967\/jnumed.112.110759","article-title":"18F-fluorobenzoate-labeled cystine knot peptides for PET imaging of integrin \u03b1v\u03b26","volume":"54","author":"Hackel","year":"2013","journal-title":"J. Nucl. Med."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"251","DOI":"10.2967\/jnumed.109.069831","article-title":"Evaluation of a 64Cu-labeled cystine-knot peptide based on agouti-related protein for PET of tumors expressing alphavbeta3 integrin","volume":"51","author":"Jiang","year":"2010","journal-title":"J. Nucl. Med."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"1232","DOI":"10.1074\/mcp.M115.055954","article-title":"Proteome-wide Identification of Novel Ceramide-binding Proteins by Yeast Surface cDNA Display and Deep Sequencing","volume":"15","author":"Bidlingmaier","year":"2016","journal-title":"Mol. Cell. Proteom."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1016\/j.sbi.2016.11.001","article-title":"Deep sequencing methods for protein engineering and design","volume":"45","author":"Wrenbeck","year":"2017","journal-title":"Curr. Opin. Struct. Biol."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"1258","DOI":"10.1016\/j.tibtech.2024.04.003","article-title":"Yeast-based screening platforms to understand and improve human health","volume":"42","author":"Deichmann","year":"2024","journal-title":"Trends Biotechnol."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/j.ymeth.2012.03.014","article-title":"Protein selection using yeast surface display","volume":"60","author":"Gera","year":"2013","journal-title":"Methods"},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"Aid-0028-2014","DOI":"10.1128\/microbiolspec.AID-0028-2014","article-title":"Phage and Yeast Display","volume":"3","author":"Sheehan","year":"2015","journal-title":"Microbiol. Spectr."},{"key":"ref_103","doi-asserted-by":"crossref","unstructured":"Bozovi\u010dar, K., and Bratkovi\u010d, T. (2019). Evolving a Peptide: Library Platforms and Diversification Strategies. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21010215"},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1093\/protein\/gzl057","article-title":"Antigen selection from an HIV-1 immune antibody library displayed on yeast yields many novel antibodies compared to selection from the same library displayed on phage","volume":"20","author":"Bowley","year":"2007","journal-title":"Protein Eng. Des. Sel."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"829","DOI":"10.1021\/ci100431r","article-title":"CycloPs: Generating virtual libraries of cyclized and constrained peptides including nonnatural amino acids","volume":"51","author":"Duffy","year":"2011","journal-title":"J. Chem. Inf. Model."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"115308","DOI":"10.1016\/j.foodres.2024.115308","article-title":"Identification and anticoagulant mechanisms of novel factor XIa inhibitory peptides by virtual screening of a in silico generated deep-sea peptide database","volume":"197","author":"Ouyang","year":"2024","journal-title":"Food Res. Int."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"169006","DOI":"10.1016\/j.jmb.2025.169006","article-title":"A combined in silico approach to design peptide ligands with increased receptor-subtype selectivity","volume":"437","author":"Zech","year":"2025","journal-title":"J. Mol. Biol."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"2683","DOI":"10.1021\/acs.jcim.5c03227","article-title":"Development and Experimental Validation of a Machine-Learning- and Physics-Based Exhaustive Hexapeptide Screening Model for Target Proteins","volume":"66","author":"He","year":"2026","journal-title":"J. Chem. Inf. Model."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"11232","DOI":"10.1021\/acs.jcim.5c01505","article-title":"Investigation into Cyclopeptide-Based Antitumor Agents: Design, Precision Synthesis, Virtual Target Screening, and Experimental Verification","volume":"65","author":"Lv","year":"2025","journal-title":"J. Chem. Inf. Model."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"W249","DOI":"10.1093\/nar\/gkr431","article-title":"Rosetta FlexPepDock web server\u2014High resolution modeling of peptide-protein interactions","volume":"39","author":"London","year":"2011","journal-title":"Nucleic Acids Res."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1007\/s11030-020-10171-6","article-title":"Designing of peptide aptamer targeting the receptor-binding domain of spike protein of SARS-CoV-2: An in silico study","volume":"26","author":"Devi","year":"2022","journal-title":"Mol. Divers."},{"key":"ref_112","doi-asserted-by":"crossref","unstructured":"Cui, J., Feng, Y., Yang, T., Wang, X., and Tang, H. (2023). Computer-Aided Designing Peptide Inhibitors of Human Hematopoietic Prostaglandin D2 Synthase Combined Molecular Docking and Molecular Dynamics Simulation. Molecules, 28.","DOI":"10.3390\/molecules28155933"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1085\/jgp.201210827","article-title":"Intermediate state trapping of a voltage sensor","volume":"140","author":"Lacroix","year":"2012","journal-title":"J. Gen. Physiol."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1038\/nmeth.4067","article-title":"CHARMM36m: An improved force field for folded and intrinsically disordered proteins","volume":"14","author":"Huang","year":"2017","journal-title":"Nat. Methods"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"2494","DOI":"10.1021\/acs.jctc.9b00251","article-title":"Development of a Force Field for the Simulation of Single-Chain Proteins and Protein-Protein Complexes","volume":"16","author":"Piana","year":"2020","journal-title":"J. Chem. Theory Comput."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"528","DOI":"10.1021\/acs.jctc.9b00591","article-title":"ff19SB: Amino-Acid-Specific Protein Backbone Parameters Trained against Quantum Mechanics Energy Surfaces in Solution","volume":"16","author":"Tian","year":"2020","journal-title":"J. Chem. Theory Comput."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1038\/s41586-021-03819-2","article-title":"Highly accurate protein structure prediction with AlphaFold","volume":"596","author":"Jumper","year":"2021","journal-title":"Nature"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"871","DOI":"10.1126\/science.abj8754","article-title":"Accurate prediction of protein structures and interactions using a three-track neural network","volume":"373","author":"Baek","year":"2021","journal-title":"Science"},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1038\/nprot.2016.169","article-title":"The ClusPro web server for protein-protein docking","volume":"12","author":"Kozakov","year":"2017","journal-title":"Nat. Protoc."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1002\/prot.25219","article-title":"New additions to the ClusPro server motivated by CAPRI","volume":"85","author":"Vajda","year":"2017","journal-title":"Proteins"},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"1731","DOI":"10.1021\/ja026939x","article-title":"HADDOCK: A protein-protein docking approach based on biochemical or biophysical information","volume":"125","author":"Dominguez","year":"2003","journal-title":"J. Am. Chem. Soc."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"720","DOI":"10.1016\/j.jmb.2015.09.014","article-title":"The HADDOCK2.2 Web Server: User-Friendly Integrative Modeling of Biomolecular Complexes","volume":"428","author":"Rodrigues","year":"2016","journal-title":"J. Mol. Biol."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1021\/acsabm.0c00707","article-title":"Self-Assembled Peptide Drug Delivery Systems","volume":"4","author":"Yang","year":"2021","journal-title":"ACS Appl. Bio Mater."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1016\/j.actbio.2021.06.027","article-title":"Cationic self-assembled peptide-based molecular hydrogels for extended ocular drug delivery","volume":"131","author":"Liu","year":"2021","journal-title":"Acta Biomater."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"114097","DOI":"10.1016\/j.addr.2021.114097","article-title":"Oral delivery of therapeutic peptides and proteins: Technology landscape of lipid-based nanocarriers","volume":"182","author":"Haddadzadegan","year":"2022","journal-title":"Adv. Drug Deliv. Rev."},{"key":"ref_126","doi-asserted-by":"crossref","unstructured":"Abed, H.F., Abuwatfa, W.H., and Husseini, G.A. (2022). Redox-Responsive Drug Delivery Systems: A Chemical Perspective. Nanomaterials, 12.","DOI":"10.3390\/nano12183183"},{"key":"ref_127","doi-asserted-by":"crossref","unstructured":"Sercombe, L., Veerati, T., Moheimani, F., Wu, S.Y., Sood, A.K., and Hua, S. (2015). Advances and Challenges of Liposome Assisted Drug Delivery. Front. Pharmacol., 6.","DOI":"10.3389\/fphar.2015.00286"},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"10938","DOI":"10.1021\/acs.chemrev.5b00046","article-title":"New Developments in Liposomal Drug Delivery","volume":"115","author":"Pattni","year":"2015","journal-title":"Chem. Rev."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"1078","DOI":"10.1038\/s41578-021-00358-0","article-title":"Lipid nanoparticles for mRNA delivery","volume":"6","author":"Hou","year":"2021","journal-title":"Nat. Rev. Mater."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"8655","DOI":"10.2147\/OTT.S186606","article-title":"A peptide-CpG-DNA-liposome complex vaccine targeting TM4SF5 suppresses growth of pancreatic cancer in a mouse allograft model","volume":"11","author":"Park","year":"2018","journal-title":"OncoTargets Ther."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1186\/s12645-023-00213-7","article-title":"Nanoliposomal VEGF-R2 peptide vaccine acts as an effective therapeutic vaccine in a murine B16F10 model of melanoma","volume":"14","author":"Zahedipour","year":"2023","journal-title":"Cancer Nanotechnol."},{"key":"ref_132","doi-asserted-by":"crossref","unstructured":"Naghibi, L., Yazdani, M., Momtazi-Borojeni, A.A., Razazan, A., Shariat, S., Mansourian, M., Arab, A., Barati, N., Arabsalmani, M., and Abbasi, A. (2020). Preparation of nanoliposomes containing HER2\/neu (P5+435) peptide and evaluation of their immune responses and anti-tumoral effects as a prophylactic vaccine against breast cancer. PLoS ONE, 15.","DOI":"10.1371\/journal.pone.0243550"},{"key":"ref_133","doi-asserted-by":"crossref","unstructured":"Bulbake, U., Doppalapudi, S., Kommineni, N., and Khan, W. (2017). Liposomal Formulations in Clinical Use: An Updated Review. Pharmaceutics, 9.","DOI":"10.3390\/pharmaceutics9020012"},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1038\/s41573-020-0090-8","article-title":"Engineering precision nanoparticles for drug delivery","volume":"20","author":"Mitchell","year":"2021","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1016\/j.actbio.2015.01.044","article-title":"Redox-responsive micelles self-assembled from dynamic covalent block copolymers for intracellular drug delivery","volume":"17","author":"Yang","year":"2015","journal-title":"Acta Biomater."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1146\/annurev-chembioeng-092319-083243","article-title":"Molecular Modeling and Simulations of Peptide-Polymer Conjugates","volume":"11","author":"Taylor","year":"2020","journal-title":"Annu. Rev. Chem. Biomol. Eng."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"e2401289","DOI":"10.1002\/adhm.202401289","article-title":"Redox-Responsive Hydrogels Loaded with an Antibacterial Peptide as Controlled Drug Delivery for Healing Infectious Wounds","volume":"13","author":"Cherri","year":"2024","journal-title":"Adv. Healthc. Mater."},{"key":"ref_138","doi-asserted-by":"crossref","unstructured":"Korovkina, O., Polyakov, D., Korzhikov-Vlakh, V., and Korzhikova-Vlakh, E. (2022). Stimuli-Responsive Polypeptide Nanoparticles for Enhanced DNA Delivery. Molecules, 27.","DOI":"10.3390\/molecules27238495"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"1461","DOI":"10.1039\/D0RA09898A","article-title":"Targeting self-assembled F127-peptide polymer with pH sensitivity for release of anticancer drugs","volume":"11","author":"Han","year":"2021","journal-title":"RSC Adv."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"837","DOI":"10.3762\/bjoc.11.93","article-title":"Peptide-polymer ligands for a tandem WW-domain, an adaptive multivalent protein-protein interaction: Lessons on the thermodynamic fitness of flexible ligands","volume":"11","author":"Koschek","year":"2015","journal-title":"Beilstein J. Org. Chem."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1016\/j.addr.2020.10.008","article-title":"Bioengineered elastin- and silk-biomaterials for drug and gene delivery","volume":"160","author":"Chambre","year":"2020","journal-title":"Adv. Drug Deliv. Rev."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"eabn4704","DOI":"10.1126\/sciadv.abn4704","article-title":"Semirational bioengineering of AAV vectors with increased potency and specificity for systemic gene therapy of muscle disorders","volume":"8","author":"Tulalamba","year":"2022","journal-title":"Sci. Adv."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"107283","DOI":"10.1016\/j.jbc.2024.107283","article-title":"Utility of protein-protein binding surfaces composed of anti-parallel alpha-helices and beta-sheets selected by phage display","volume":"300","author":"Zhu","year":"2024","journal-title":"J. Biol. Chem."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"694","DOI":"10.1038\/gt.2012.20","article-title":"Directed evolution of novel adeno-associated viruses for therapeutic gene delivery","volume":"19","author":"Bartel","year":"2012","journal-title":"Gene Ther."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"204","DOI":"10.1038\/nbt.3440","article-title":"Cre-dependent selection yields AAV variants for widespread gene transfer to the adult brain","volume":"34","author":"Deverman","year":"2016","journal-title":"Nat. Biotechnol."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"1139","DOI":"10.1126\/science.aaw2900","article-title":"Comprehensive AAV capsid fitness landscape reveals a viral gene and enables machine-guided design","volume":"366","author":"Ogden","year":"2019","journal-title":"Science"},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1097\/COH.0000000000000524","article-title":"Human cytomegalovirus-vectored vaccines against HIV","volume":"14","author":"Goonetilleke","year":"2019","journal-title":"Curr. Opin. HIV AIDS"},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"113818","DOI":"10.1016\/j.addr.2021.05.028","article-title":"Antimicrobial peptides towards clinical application: Delivery and formulation","volume":"175","author":"Wang","year":"2021","journal-title":"Adv. Drug Deliv. Rev."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"e3011","DOI":"10.1002\/jgm.3011","article-title":"Polymer-coated viral vectors: Hybrid nanosystems for gene therapy","volume":"20","author":"Rajagopal","year":"2018","journal-title":"J. Gene Med."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"3640","DOI":"10.1039\/C7CS00817A","article-title":"Solid-state electrical applications of protein and peptide based nanomaterials","volume":"47","author":"Panda","year":"2018","journal-title":"Chem. Soc. Rev."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1016\/j.bios.2018.12.005","article-title":"Peptide-modified electrolyte-gated organic field effect transistor. Application to Cu2+ detection","volume":"127","author":"Nguyen","year":"2019","journal-title":"Biosens. Bioelectron."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"103066","DOI":"10.1016\/j.sbi.2025.103066","article-title":"Artificial intelligencemethods for protein folding and design","volume":"93","author":"Zhang","year":"2025","journal-title":"Curr. Opin. Struct. Biol."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1038\/nrd1632","article-title":"Recent advances with liposomes as pharmaceutical carriers","volume":"4","author":"Torchilin","year":"2005","journal-title":"Nat. Rev. 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