Structural properties of bioactive peptides with α-glucosidase inhibitory activity

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dc.contributor.author Ibrahim, Mohammed Auwal
dc.contributor.author Bester, Megan Jean
dc.contributor.author Neitz, A.W.H. (Albert Walter Herman)
dc.contributor.author Gaspar, A.R.M. (Anabella Regina Marques)
dc.date.accessioned 2017-10-26T08:45:33Z
dc.date.issued 2018-02
dc.description.abstract Bioactive peptides are emerging as promising class of drugs that could serve as α-glucosidase inhibitors for the treatment of type 2 diabetes. This article identifies structural and physicochemical requirements for the design of therapeutically relevant α-glucosidase inhibitory peptides. So far, a total of 43 fully sequenced α-glucosidase inhibitory peptides have been reported and 13 of them had IC50 values several folds lower than acarbose. Analysis of the peptides indicates that the most potent peptides are tri- to hexapeptides with amino acids containing a hydroxyl or basic side chain at the N-terminal. The presence of proline within the chain and alanine or methionine at the C-terminal appears to be relevant for high activity. Hydrophobicity and isoelectric points are less important variables for α-glucosidase inhibition whilst a net charge of 0 or +1 was predicted for the highly active peptides. In silico simulated gastrointestinal digestion revealed that the high and moderately active peptides, including the most potent peptide (STYV), were gastrointestinally unstable, except SQSPA. Molecular docking of SQSPA, STYV, and STY (digestion fragment of STYV) with α-glucosidase suggested that their hydrogen bonding interactions and binding energies were comparable with acarbose. The identified criteria will facilitate the design of new peptide-derived α-glucosidase inhibitors. en_ZA
dc.description.department Anatomy en_ZA
dc.description.department Biochemistry en_ZA
dc.description.embargo 2019-02-18
dc.description.librarian hj2017 en_ZA
dc.description.sponsorship The National Research Foundation of South Africa and the University of Pretoria. The first author also acknowledges the University of Pretoria for the award of a postdoctoral fellowship position in Biochemistry and Ahmadu Bello University, Zaria, Nigeria for the award of a study fellowship. en_ZA
dc.description.uri http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1747-0285 en_ZA
dc.description.uri http://wileyonlinelibrary.com/journal/cbdd en_ZA
dc.identifier.citation Ibrahim, M.A., Bester, M.J., Neitz, A.W.H. & Gaspar, A.R.M. 2018, 'Structural properties of bioactive peptides with α-glucosidase inhibitory activity', Chemical Biology and Drug Design, vol. 91, no. 2, pp. 370-379 en_ZA
dc.identifier.issn 1747-0277 (print)
dc.identifier.issn 1747-0285 (online)
dc.identifier.other 10.1111/cbdd.13105
dc.identifier.uri http://hdl.handle.net/2263/62941
dc.language.iso en en_ZA
dc.publisher Wiley en_ZA
dc.rights © 2017 John Wiley & Sons A/S. This is the pre-peer reviewed version of the following article : 'Structural properties of bioactive peptides with α-glucosidase inhibitory activity', Chemical Biology and Drug Design, vol. 91, no. 2, pp. 370-379, 2018, doi : 10.1111/cbdd.13105. The definite version is available at : http://onlinelibrary.wiley.comjournal/10.1111/(ISSN)1747-0285. en_ZA
dc.subject Amino acid (AA) en_ZA
dc.subject Bioactive peptides en_ZA
dc.subject Physicochemical properties en_ZA
dc.subject Type 2 diabetes (T2D) en_ZA
dc.subject α-glucosidase en_ZA
dc.title Structural properties of bioactive peptides with α-glucosidase inhibitory activity en_ZA
dc.type Postprint Article en_ZA


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