Characterization of Peptides from Capsicum annuum Hybrid Seeds with Inhibitory Activity Against [alpha]-Amylase, Serine Proteinases and Fungi

• Published in: The Protein Journal Vol. 34; no. 2; p. 122
• Main Authors: Vieira Bard, Gabriela C, Nascimento, Viviane V, Ribeiro, Suzanna F. F, Rodrigues, Rosana, Perales, Jonas, Teixeira-Ferreira, André, Carvalho, André O
• Format: Journal Article
• Language: English
• Published: New York Springer 01.04.2015; Springer Nature B.V
• Subjects: Amino acids; Ammonium; Ammonium compounds; Ammonium paratungstate; Amylases; Antimicrobial agents; Fungi; Mass spectrometry; Microorganisms; Peptides; Plant species; Protease inhibitors; Proteases; Proteinase inhibitors; Proteins; Seeds; Serine; Sulfates; Yeasts
• ISSN: 1572-3887; 1875-8355; 1573-4943
• DOI: 10.1007/s10930-015-9604-3

Over the last several years, the activity of antimicrobial peptides (AMPs), isolated from plant species, against different microorganisms has been demonstrated. More recently, some of these AMPs have been described as potent inhibitors of [alpha]-amylases and serine proteinases from insects and mammals. The aim of this work was to obtain AMPs from protein extracts of a hybrid Capsicum (Ikeda x UENF 1381) seeds and to evaluate their microbial and enzyme inhibitory activities. Initially, proteins were extracted from the Capsicum hybrid seeds in buffer (sodium phosphate pH 5.4,) and precipitated with ammonium sulfate (90 % saturated). Extract of hybrid seeds was subjected to size exclusion chromatography, and three fractions were obtained: S1, S2 and S3. The amino acid sequence, obtained by mass spectrometry, of the 6 kDa peptide from the S3 fraction, named HyPep, showed 100 % identity with PSI-1.2, a serine protease inhibitor isolated from C. annuum seeds, however the bifunctionality of this inhibitor against two enzymes is being shown for the first time in this work. The S3 fraction showed the highest antifungal activity, inhibiting all the yeast strains tested, and it also exhibited inhibitory activity against human salivary and Callosobruchus maculatus [alpha]-amylases as well as serine proteinases.