Journal of Agricultural and Food Chemistry: Latest Articles (ACS Publications)

Journal of Agricultural and Food Chemistry: Latest Articles (ACS Publications)

Structure-Based Identification and Design of Angiotensin Converting Enzyme-Inhibitory Peptides from Whey Proteins Anna Rita Tondo Anna Rita Tondo Department of Pharmacy-Drug Sciences, University of Studies of Bari Aldo Moro, Via E. Orabona, 4, 70126 Bari, Italy Leonardo Caputo Leonardo Caputo Institute of Sciences of Food Production (CNR-ISPA) National Council of Research, Via G. Amendola, 122/O, 70126 Bari, Italy Linda Monaci Linda Monaci Institute of Sciences of Food Production (CNR-ISPA) National Council of Research, Via G. Amendola, 122/O, 70126 Bari, Italy Giovanni Lentini Giovanni Lentini Department of Pharmacy-Drug Sciences, University of Studies of Bari Aldo Moro, Via E. Orabona, 4, 70126 Bari, Italy Antonio Francesco Logrieco Antonio Francesco Logrieco Institute of Sciences of Food Production (CNR-ISPA) National Council of Research, Via G. Amendola, 122/O, 70126 Bari, Italy Michele Montaruli Michele Montaruli Department of Pharmacy-Drug Sciences, University of Studies of Bari Aldo Moro, Via E. Orabona, 4, 70126 Bari, Italy Orazio Nicolotti * Orazio Nicolotti Department of Pharmacy-Drug Sciences, University of Studies of Bari Aldo Moro, Via E. Orabona, 4, 70126 Bari, Italy Laura Quintieri * Laura Quintieri Institute of Sciences of Food Production (CNR-ISPA) National Council of Research, Via G. Amendola, 122/O, 70126 Bari, Italy * Phone: +39 080.5929323. Fax: +39 080 5929373. E-mail: [email protected] . Cite this: J. Agric. Food Chem. 2019 , XXXX , XXX , XXX-XXX Publication Date (Web) : December 20, 2019 Publication History LEARN ABOUT THESE METRICS Article Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days. Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts. The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Get e-Alerts Abstract Besides their nutritional value, whey protein (WP) peptides are food components retaining important pharmacological properties for controlling hypertension. We herein report how the use of complementary experimental and theoretical investigations allowed the identification of novel angiotensin converting enzyme inhibitory (ACEI) peptides obtained from a WP hydrolysate and addressed the rational design of even shorter sequences based on molecular pruning. Thus, after bromelain digestion followed by a 5 kDa cutoff ultrafiltration, WP hydrolysate with ACEI activity was fractioned by RP-HPLC; 2 out of 23 collected fractions retained ACEI activity and were analyzed by liquid chromatography–tandem mass spectrometry (LC–MS/MS). In the face of 128 identified peptides, molecular docking was carried out to prioritize peptides and to rationally guide the design of novel shorter and bioactive sequences. Therefore, 11 peptides, consisting of 3–6 amino acids and with molecular weights in the range from 399 to 674 Da, were rationally designed and then purchased to determine the IC 50 value. This approach allowed the identification of two novel peptides: MHI and IAEK with IC 50 ACEI values equal to 11.59 and 25.08 μM, respectively. Interestingly, we also confirmed the well-known ACEI IPAVF with an IC 50 equal to 9.09 μM. In light of these results, this integrated approach could pave the way for high-throughput screening and identification of new peptides in dairy products. In addition, the herein proposed ACEI peptides could be exploited for novel applications both for food production and pharmaceuticals. KEYWORDS:



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