{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,10]],"date-time":"2026-10-10T00:05:56Z","timestamp":1791590756240,"version":"4.3.4"},"reference-count":41,"publisher":"MDPI AG","issue":"11","license":[{"start":{"date-parts":[[2020,11,23]],"date-time":"2020-11-23T00:00:00Z","timestamp":1606089600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Nutrients"],"abstract":"<jats:p>Recent studies continue to demonstrate the potential of edible insects as a protein base to obtain bioactive peptides applicable for functional food development. This study aimed at identifying antihypertensive, anti-glycemic, and anti-inflammatory peptides derived from the in vitro gastrointestinal digests of cricket protein hydrolysates. After sequential fractionation, the protein digest subfraction containing the lowest molecular weight (&lt;0.5 kDa), hydrophobic (C18) and cationic peptides (IEX) was found responsible for the most bioactivity. The cationic peptide fraction significantly reduced (p &lt; 0.05) \u03b1-amylase, \u03b1-glucosidase, and angiotensin converting enzyme (ACE) activity in vitro, and also inhibited the expression of NF-\u03baB in RAW 264.7 macrophage cells. A total of 28 peptides were identified with mass spectrometry (LC\u2013MS\/MS) and de novo sequencing from the potent fraction. Three novel peptides YKPRP, PHGAP, and VGPPQ were chosen for the molecular docking studies. PHGAP and VGPPQ exhibited a higher degree of non-covalent interactions with the enzyme active site residues and binding energies comparable to captopril. Results from this study demonstrate the bioactive potential of edible cricket peptides, especially as ACE inhibitors.<\/jats:p>","DOI":"10.3390\/nu12113588","type":"journal-article","created":{"date-parts":[[2020,11,23]],"date-time":"2020-11-23T08:18:23Z","timestamp":1606119503000},"page":"3588","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":85,"title":["Identification and Characterization of Edible Cricket Peptides on Hypertensive and Glycemic In Vitro Inhibition and Their Anti-Inflammatory Activity on RAW 264.7 Macrophage Cells"],"prefix":"10.3390","volume":"12","author":[{"given":"Felicia","family":"Hall","sequence":"first","affiliation":[{"name":"Protein Chemistry and Bioactive Peptides Laboratory, Purdue University, West Lafayette, IN 47907, USA"},{"name":"Department of Food Science, Purdue University, 745 Agriculture Drive, West Lafayette, IN 47907, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lavanya","family":"Reddivari","sequence":"additional","affiliation":[{"name":"Department of Food Science, Purdue University, 745 Agriculture Drive, West Lafayette, IN 47907, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0994-1205","authenticated-orcid":false,"given":"Andrea M.","family":"Liceaga","sequence":"additional","affiliation":[{"name":"Protein Chemistry and Bioactive Peptides Laboratory, Purdue University, West Lafayette, IN 47907, USA"},{"name":"Department of Food Science, Purdue University, 745 Agriculture Drive, West Lafayette, IN 47907, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2020,11,23]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1","DOI":"10.7326\/0003-4819-145-1-200607040-00004","article-title":"Effects of a Mediterranean-Style Diet on Cardiovascular Risk Factors: A randomized trial","volume":"145","author":"Estruch","year":"2006","journal-title":"Ann. 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