Colostrum is essential for the survival and development of newborn mammals. This primary source of nourishment during the first days of infant life is rich in functional components conductive to the enhancement of neonate immunity and growth. Compared with mature milk, a higher protein and peptide content is observed in colostrum, whilst it is low in fat and carbohydrates. The functional properties of colostrum are closely linked to the release of bioactive peptides during the gastrointestinal digestion of colostrum proteins. Our study aimed to comprehensively analyze the whey proteome of colostrum from indigenous Greek goats and to examine the influence of bioactive peptides released during digestion on human metabolism. Colostrum and mature milk samples from healthy ewes were subjected to nanoLC-MS/MS analysis, revealing differentially expressed proteins. These proteins were functionally characterized and subjected to in silico digestion. Using machine learning models, we classified the peptide functional groups, while molecular docking assessed the binding affinity of the proposed angiotensin-converting enzyme (ACE)- and dipeptidyl peptidase IV (DPPIV)-inhibitory peptides to their target molecules. A total of 898 proteins were identified in colostrum, 40 of which were overexpressed compared with mature milk. The enzymatic cleavage of upregulated proteins by key gastrointestinal tract proteases and the downstream analysis of peptide sequences identified 117 peptides predicted (with >80% confidence) to impact metabolism, primarily through modulation of the renin-angiotensin system, insulin secretion, and redox pathways. This work advances our understanding of dietary bioactive peptides and their relevance to human metabolism, highlighting the potential health benefits of colostrum consumption.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.3390/foods13233949 | DOI Listing |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11640771 | PMC |
JACS Au
December 2024
Laboratory of Bioorganic Chemistry, National Institutes of Diabetes, Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892, United States.
Methods that enable the on-demand synthesis of biologically active molecules offer the potential for a high degree of control over the timing and context of target activation; however, such approaches often require extensive engineering to implement. Tools to restrict the localization of assembly also remain limited. Here we present a new approach for stimulus-induced ligand assembly that helps to address these challenges.
View Article and Find Full Text PDFBioact Mater
April 2025
Department of Oral and Cranio-maxillofacial Surgery, Shanghai Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine; College of Stomatology, Shanghai Jiao Tong University; National Center for Stomatology; National Clinical Research Center for Oral Diseases; Shanghai Key Laboratory of Stomatology; Shanghai Research Institute of Stom, Shanghai, 200011, China.
Angiogenesis is imperative for bone regeneration, yet the conventional cytokine therapies have been constrained by prohibitive costs and safety apprehensions. It is urgent to develop a safer and more efficient therapeutic alternative. Herein, utilizing the methodologies of Deep Learning (DL) and Natural Language Processing (NLP), we proposed a paradigm algorithm that amalgamates with a variant, , to deftly discern potential pro-angiogenic peptides from intrinsically disordered regions (IDRs) of 262 related proteins, where are fertile grounds for developing safer and highly promising bioactive peptides.
View Article and Find Full Text PDFJ Biol Chem
December 2024
Department of Biosystems Science, Institute for Life and Medical Sciences, Kyoto University, Kyoto 606-8507, Japan; Department of Mammalian and Regulatory Networks, Graduate School of Biostudies, Kyoto University, Kyoto 606-8502, Japan; Department of Homeostatic Medicine, Medical Research Laboratory, Institute of Integrated Research, Institute of Science Tokyo, Yushima Bunkyo-ku, Tokyo 113-8510, Japan. Electronic address:
Alpha-1-antitrypsin (AAT), a circulating serine protease inhibitor, is an acute inflammatory response protein with anti-inflammatory functions. The C-terminal peptides of AAT are found in various tissues and have been proposed as putative bioactive peptides with multiple functions, but its mechanism of action remains unclear. We previously reported that a mouse AAT C-terminal peptide of 35 amino acids (mAAT-C) penetrates plasma membrane and associates guanine nucleotide-binding protein subunit alpha 13 (Gα13).
View Article and Find Full Text PDFPoult Sci
December 2024
Animal Breeding and Genetics key Laboratory of Sichuan Province, Sichuan Animal Science Academy, Chengdu 610066, PR China. Electronic address:
This study aimed to investigate the effects of soybean bioactive peptide (SBP) on the growth performance and intestinal health of yellow-feathered broilers and to further elucidate the regulatory mechanisms of intestinal health using multi-omics analysis. A total of 320 1-day-old yellow-feathered broilers were randomly divided into two groups, with 10 replicates per group and 16 birds per replicate. Broilers in the control group received the basal diet, and those in the experimental group (SBPG) received the basal diet with 0.
View Article and Find Full Text PDFUltrason Sonochem
December 2024
Shenzhen Key Laboratory of Food Nutrition and Health, Guangdong Engineering Technology Research Center of Aquatic Food Processing and Safety Control, School of Chemistry and Environmental Engineering, Shenzhen University, Shenzhen 518060, China. Electronic address:
In this study, the effects of ultrasound-assisted enzymatic hydrolysis on the production of antioxidant and antiosteoporotic peptides derived from oysters were investigated. Results showed that ultrasound-assisted enzymatic hydrolysis significantly enhanced the peptide content, free radical scavenging ability, and ferric reducing antioxidant power of total oyster protein hydrolysate (TOPH), with optimal results achieved at 200 W (TOPH-200). Correspondingly, ultrasound treatment at 200 W increased the exposure of hydrophobic regions, reduced α-helix content, and facilitated the generation of small molecular weight peptides in TOPH.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!