{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,10]],"date-time":"2026-09-10T03:37:01Z","timestamp":1789011421523,"version":"build-2803163510"},"reference-count":40,"publisher":"MDPI AG","issue":"4","license":[{"start":{"date-parts":[[2018,4,10]],"date-time":"2018-04-10T00:00:00Z","timestamp":1523318400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Polymers"],"abstract":"<jats:p>The functionalization of polymer surfaces by polymer-binding peptides offers tremendous opportunities for directed immobilization of enzymes, bioactive peptides, and antigens. The application of polymer-binding peptides as adhesion promoters requires reliable and stable binding under process conditions. Molecular modes of interactions between material surfaces, peptides, and solvent are often not understood to an extent that enables (semi-) rational design of polymer-binding peptides, hindering the full exploitation of their potential. Knowledge-gaining directed evolution (KnowVolution) is an efficient protein engineering strategy that facilitates tailoring protein properties to application demands through a combination of directed evolution and computational guided protein design. A single round of KnowVolution was performed to gain molecular insights into liquid chromatography peak I peptide, 47 aa (LCI)-binding to polypropylene (PP) in the presence of the competing surfactant Triton X-100. KnowVolution yielded a total of 8 key positions (D19, S27, Y29, D31, G35, I40, E42, and D45), which govern PP-binding in the presence of Triton X-100. The recombination of two of the identified amino acid substitutions (Y29R and G35R; variant KR-2) yielded a 5.4 \u00b1 0.5-fold stronger PP-binding peptide compared to LCI WT in the presence of Triton X-100 (1 mM). The LCI variant KR-2 shows a maximum binding capacity of 8.8 \u00b1 0.1 pmol\/cm2 on PP in the presence of Triton X-100 (up to 1 mM). The KnowVolution approach enables the development of polymer-binding peptides, which efficiently coat and functionalize PP surfaces and withstand surfactant concentrations that are commonly used, such as in household detergents.<\/jats:p>","DOI":"10.3390\/polym10040423","type":"journal-article","created":{"date-parts":[[2018,4,10]],"date-time":"2018-04-10T13:06:08Z","timestamp":1523365568000},"page":"423","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":68,"title":["KnowVolution of the Polymer-Binding Peptide LCI for Improved Polypropylene Binding"],"prefix":"10.3390","volume":"10","author":[{"given":"Kristin","family":"R\u00fcbsam","sequence":"first","affiliation":[{"name":"Institute of Biotechnology, RWTH Aachen University, Worringerweg 3, D-52074 Aachen, Germany"},{"name":"DWI\u2014Leibniz-Institute for Interactive Materials, Forckenbeckstrasse 50, D-52074 Aachen, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mehdi","family":"Davari","sequence":"additional","affiliation":[{"name":"Institute of Biotechnology, RWTH Aachen University, Worringerweg 3, D-52074 Aachen, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Felix","family":"Jakob","sequence":"additional","affiliation":[{"name":"DWI\u2014Leibniz-Institute for Interactive Materials, Forckenbeckstrasse 50, D-52074 Aachen, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ulrich","family":"Schwaneberg","sequence":"additional","affiliation":[{"name":"Institute of Biotechnology, RWTH Aachen University, Worringerweg 3, D-52074 Aachen, Germany"},{"name":"DWI\u2014Leibniz-Institute for Interactive Materials, Forckenbeckstrasse 50, D-52074 Aachen, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2018,4,10]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"5065","DOI":"10.1021\/acs.langmuir.7b00441","article-title":"Oriented Coimmobilization of Oxidase and Catalase on Tailor-Made Ordered Mesoporous Silica","volume":"33","author":"Bolivar","year":"2017","journal-title":"Langmuir"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"5124","DOI":"10.1021\/acsami.5b11949","article-title":"Modification of Titanium Substrates with Chimeric Peptides Comprising Antimicrobial and Titanium-Binding Motifs Connected by Linkers To Inhibit Biofilm Formation","volume":"8","author":"Liu","year":"2016","journal-title":"ACS Appl. Mater. Interface"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1016\/j.tibtech.2015.02.005","article-title":"Solid-binding peptides: Smart tools for nanobiotechnology","volume":"33","author":"Care","year":"2015","journal-title":"Trends Biotechnol."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"1090","DOI":"10.1021\/acs.bioconjchem.6b00074","article-title":"Peptide-Mediated Specific Immobilization of Catalytically Active Cytochrome P450 BM3 Variant","volume":"27","author":"Zernia","year":"2016","journal-title":"Bioconjugate Chem."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"496","DOI":"10.1038\/nmat1397","article-title":"Biomaterials functionalization using a novel peptide that selectively binds to a conducting polymer","volume":"4","author":"Sanghvi","year":"2005","journal-title":"Nat. Mater."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"3651","DOI":"10.1039\/C6TB00624H","article-title":"Surface functionalization of polymer substrates with hydroxyapatite using polymer-binding peptides","volume":"4","author":"Iijima","year":"2016","journal-title":"J. Mater. Chem. B"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"13780","DOI":"10.1021\/ja054402o","article-title":"A peptide motif recognizing a polymer stereoregularity","volume":"127","author":"Serizawa","year":"2005","journal-title":"J. Am. Chem. Soc."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"11127","DOI":"10.1021\/la701822n","article-title":"Highly specific affinities of short peptides against synthetic polymers","volume":"23","author":"Serizawa","year":"2007","journal-title":"Langmuir"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"17278","DOI":"10.1021\/la102018f","article-title":"Biological Identification of Peptides that Specifically Bind to Poly(phenylene vinylene) Surfaces: Recognition of the Branched or Linear Structure of the Conjugated Polymer","volume":"26","author":"Ejima","year":"2010","journal-title":"Langmuir"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"3082","DOI":"10.1016\/j.msec.2013.02.011","article-title":"Recognition of epoxy with phage displayed peptides","volume":"33","author":"Swaminathan","year":"2013","journal-title":"Mat. Sci. Eng. C Mater."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"12440","DOI":"10.1021\/la801468c","article-title":"Effect of Molecular Conformations on the Adsorption Behavior of Gold-Binding Peptides","volume":"24","author":"Hnilova","year":"2008","journal-title":"Langmuir"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1016\/j.ab.2004.09.048","article-title":"The nature of target-unrelated peptides recovered in the screening of phage-displayed random peptide libraries with antibodies","volume":"336","author":"Menendez","year":"2005","journal-title":"Anal. Biochem."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/0378-1119(95)00058-E","article-title":"Characterization of Phage That Bind Plastic from Phage-Displayed Random Peptide Libraries","volume":"156","author":"Adey","year":"1995","journal-title":"Gene"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"10252","DOI":"10.1039\/c1jm10602c","article-title":"Specific interfaces between synthetic polymers and biologically identified peptides","volume":"21","author":"Serizawa","year":"2011","journal-title":"J. Mater. Chem."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"6399","DOI":"10.1021\/la8008442","article-title":"Biological selection of peptides for poly(L-lactide) substrates","volume":"24","author":"Matsuno","year":"2008","journal-title":"Langmuir"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/j.ab.2012.02.013","article-title":"HWGMWSY, an unanticipated polystyrene binding peptide from random phage display libraries","volume":"424","author":"Vodnik","year":"2012","journal-title":"Anal. Biochem."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1002\/bit.26481","article-title":"Directed evolution of polypropylene and polystyrene binding peptides","volume":"115","author":"Rubsam","year":"2018","journal-title":"Biotechnol. Bioeng."},{"key":"ref_18","unstructured":"Cunningham, S.D., Lowe, D.J., O\u2019Brien, J.P., Wang, H., and Wilkins, A.E. (2011). Polypropylene Binding Peptides and Methods of Use. (7928076B2), U.S. Patent."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1016\/j.polymer.2017.03.070","article-title":"Anchor peptides: A green and versatile method for polypropylene functionalization","volume":"116","author":"Stomps","year":"2017","journal-title":"Polymer"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1002\/bit.20149","article-title":"Identification and characterization of Cu2O- and ZnO-binding polypeptides by Escherichia coli cell surface display: Toward an understanding of metal oxide binding","volume":"87","author":"Thai","year":"2004","journal-title":"Biotechnol. Bioeng."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"312","DOI":"10.1016\/j.copbio.2007.04.008","article-title":"Selection and analysis of solid-binding peptides","volume":"18","author":"Baneyx","year":"2007","journal-title":"Curr. Opin. Biotech."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"2598","DOI":"10.1016\/j.bmcl.2013.02.106","article-title":"Identification of metal ion binding peptides containing unnatural amino acids by phage display","volume":"23","author":"Day","year":"2013","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"3621","DOI":"10.1021\/bi200123w","article-title":"Solution Structure of LCI, a Novel Antimicrobial Peptide from Bacillus subtilis","volume":"50","author":"Gong","year":"2011","journal-title":"Biochemistry"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"9728","DOI":"10.1021\/jp0608426","article-title":"Thermodynamic insights into the binding of triton X-100 to globular proteins: A calorimetric and spectroscopic investigation","volume":"110","author":"Singh","year":"2006","journal-title":"J. Phys. Chem. B"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"Artn-032713","DOI":"10.1103\/PhysRevE.92.032713","article-title":"Tuning of protein-surfactant interaction to modify the resultant structure","volume":"92","author":"Mehan","year":"2015","journal-title":"Phys. Rev. E"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"2842","DOI":"10.1073\/pnas.0707879105","article-title":"Peptide adsorption on a hydrophobic surface results from an interplay of solvation, surface, and intrapeptide forces","volume":"105","author":"Horinek","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1016\/j.bios.2013.06.029","article-title":"Reengineered glucose oxidase for amperometric glucose determination in diabetes analytics","volume":"50","author":"Gutierrez","year":"2013","journal-title":"Biosens. Bioelectron."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"9760","DOI":"10.1039\/C5CC01594D","article-title":"Directed evolution 2.0: Improving and deciphering enzyme properties","volume":"51","author":"Cheng","year":"2015","journal-title":"Chem. Commun."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"2719","DOI":"10.1039\/c2gc35790a","article-title":"Reengineering CelA2 cellulase for hydrolysis in aqueous solutions of deep eutectic solvents and concentrated seawater","volume":"14","author":"Lehmann","year":"2012","journal-title":"Green Chem."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"711","DOI":"10.1002\/bit.24766","article-title":"Increasing activity and thermal resistance of Bacillus gibsonii alkaline protease (BgAP) by directed evolution","volume":"110","author":"Martinez","year":"2013","journal-title":"Biotechnol. Bioeng."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"680","DOI":"10.2144\/99264st03","article-title":"Two-stage PCR protocol allowing introduction of multiple mutations, deletions and insertions using QuikChange (TM) site-directed mutagenesis","volume":"26","author":"Wang","year":"1999","journal-title":"Biotechniques"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"S136","DOI":"10.1101\/gr.3.6.S136","article-title":"Mutagenic Pcr","volume":"3","author":"Cadwell","year":"1994","journal-title":"PCR Meth. Appl."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1016\/j.jbiosc.2009.11.005","article-title":"Characterization of polystyrene-binding peptides (PS-tags) for site-specific immobilization of proteins","volume":"109","author":"Kumada","year":"2010","journal-title":"J. Biosci. Bioeng."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1016\/j.ab.2016.08.013","article-title":"A polystyrene binding target-unrelated peptide isolated in the screening of phage display library","volume":"512","author":"Bakhshinejad","year":"2016","journal-title":"Anal. Biochem."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"11347","DOI":"10.1021\/la702414m","article-title":"Conformational control of inorganic adhesion in a designer protein engineered for cuprous oxide binding","volume":"23","author":"Choe","year":"2007","journal-title":"Langmuir"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"1578","DOI":"10.1021\/cm071515t","article-title":"Identification and design of peptides for the rapid, high-yield formation of nanoparticulate TiO2 from aqueous solutions at room temperature","volume":"20","author":"Dickerson","year":"2008","journal-title":"Chem. Mater."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"10040","DOI":"10.1021\/la3012348","article-title":"Positively Charged Mini-Protein Z(basic2) As a Highly Efficient Silica Binding Module: Opportunities for Enzyme Immobilization on Unmodified Silica Supports","volume":"28","author":"Bolivar","year":"2012","journal-title":"Langmuir"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"10446","DOI":"10.1021\/la301401v","article-title":"Adsorption of Antimicrobial Indolicidin-Derived Peptides on Hydrophobic Surfaces","volume":"28","author":"Tsai","year":"2012","journal-title":"Langmuir"},{"key":"ref_39","doi-asserted-by":"crossref","unstructured":"Dennig, A., Shivange, A.V., Marienhagen, J., and Schwaneberg, U. (2011). OmniChange: The sequence independent method for simultaneous site-saturation of five codons. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0026222"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1016\/j.jbiotec.2012.02.010","article-title":"Screening of PC and PMMA-binding peptides for site-specific immobilization of proteins","volume":"160","author":"Kumada","year":"2012","journal-title":"J. Biotechnol."}],"container-title":["Polymers"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2073-4360\/10\/4\/423\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T15:00:10Z","timestamp":1760194810000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2073-4360\/10\/4\/423"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,4,10]]},"references-count":40,"journal-issue":{"issue":"4","published-online":{"date-parts":[[2018,4]]}},"alternative-id":["polym10040423"],"URL":"https:\/\/doi.org\/10.3390\/polym10040423","relation":{},"ISSN":["2073-4360"],"issn-type":[{"value":"2073-4360","type":"electronic"}],"subject":[],"published":{"date-parts":[[2018,4,10]]}}}