Journal
JOURNAL OF MOLECULAR STRUCTURE
Volume 1040, Issue -, Pages 164-170Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.molstruc.2013.03.004
Keywords
Structural diversity; Tripeptide; Molecular modeling; Food additive
Categories
Funding
- National Science 82 Technology Pillar Program [2012BAD31808]
- Foundation for Returned Overseas Chinese Scholars, State Education Ministry
- Hunan Provincial Natural Science Foundation [11JJ6025]
- Hunan Provincial Key Scientific Research Programs [2010FJ1007]
- Construct Program of the Key Discipline in Hunan Province, China
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Multifunctional peptides have attracted increasing attention in the food science community because of their therapeutic potential, low toxicity and rapid intestinal absorption. However, previous study demonstrated that the limited structural variations make it difficult to optimize dipeptide molecules in a good balance between desirable and undesirable properties (F. Tian, P. Zhou, F. Lv, R. Song, Z. Li, J. Pept. Sci. 13 (2007) 549-566). In the present work, we attempt to answer whether the structural diversity is sufficient for a tripeptide to have satisfactory multiple bioactivities. Statistical test, structural examination and energetic analysis confirm that peptides of three amino acids long can bind tightly to human angiotensin converting enzyme (ACE) and thus exert significant antihypertensive efficacy. Further quantitative structure-activity relationship (QSAR) modeling and prediction of all 8000 possible tripeptides reveal that their ACE-inhibitory potency exhibits a good (positive) relationship to antioxidative activity, but has only a quite modest correlation with bitterness. This means that it is possible to find certain tripeptide entities possessing the optimal combination of strong ACE-inhibitory potency, high antioxidative activity and weak bitter taste, which are the promising candidates for developing multifunctional food additives with satisfactory multiple bioactivities. The marked difference between dipeptide and tripeptide can be attributed to the fact that the structural diversity of peptides increases dramatically with a slight change in sequence length. (C) 2013 Elsevier B.V. All rights reserved.
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