Antimicrobial activity of antihypertensive food-derived peptides and selected alanine analogues

Stephen McClean, Louise B Beggs, Rob Welch

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

This study evaluated four food-derived peptides with known antihypertensive activities for antimicrobial activity against pathogenic microorganisms, and assessed structure-function relationships using alanine analogues. The peptides (EVSLNSGYY, barley; PGTAVFK, soybean; TTMPLW, α-casein; VHLPP, α-zein) and the six alanine substitution peptides of PGTAVFK were synthesised, characterised and evaluated for antimicrobial activity using the bacteria, E. coli, S. aureus, and M. luteus and the yeast, C. albicans. The peptides TTMPLW and PGTAVFK inhibited growth of all four microorganisms tested, with activities of a similar order of magnitude to ampicillin and ethanol controls. EVSLNSGYY inhibited the growth of the bacteria, but VHLPP showed no antimicrobial activity. The alanine analogue, PGAAVFK showed the highest overall antimicrobial activity and PGTAVFA showed no activity; overall, the activities of the analogues were consistent with their structures. Some peptides with antihypertensive activity also show antimicrobial activity, suggesting that food-derived peptides may exert beneficia1 effects via a number of mechanisms.
LanguageEnglish
Pages443-447
JournalFood Chemistry
Volume146
DOIs
Publication statusPublished - 17 Jan 2014

Fingerprint

antihypertensive effect
Alanine
alanine
Antihypertensive Agents
anti-infective agents
peptides
Food
Peptides
Microorganisms
Bacteria
alpha-zein
Zein
alpha-casein
microorganisms
bacteria
structure-activity relationships
Hordeum
Ampicillin
ampicillin
Growth

Cite this

@article{532b506ff29244339622aa04e9fd5796,
title = "Antimicrobial activity of antihypertensive food-derived peptides and selected alanine analogues",
abstract = "This study evaluated four food-derived peptides with known antihypertensive activities for antimicrobial activity against pathogenic microorganisms, and assessed structure-function relationships using alanine analogues. The peptides (EVSLNSGYY, barley; PGTAVFK, soybean; TTMPLW, α-casein; VHLPP, α-zein) and the six alanine substitution peptides of PGTAVFK were synthesised, characterised and evaluated for antimicrobial activity using the bacteria, E. coli, S. aureus, and M. luteus and the yeast, C. albicans. The peptides TTMPLW and PGTAVFK inhibited growth of all four microorganisms tested, with activities of a similar order of magnitude to ampicillin and ethanol controls. EVSLNSGYY inhibited the growth of the bacteria, but VHLPP showed no antimicrobial activity. The alanine analogue, PGAAVFK showed the highest overall antimicrobial activity and PGTAVFA showed no activity; overall, the activities of the analogues were consistent with their structures. Some peptides with antihypertensive activity also show antimicrobial activity, suggesting that food-derived peptides may exert beneficia1 effects via a number of mechanisms.",
author = "Stephen McClean and Beggs, {Louise B} and Rob Welch",
year = "2014",
month = "1",
day = "17",
doi = "10.1016/j.foodchem.2013.09.094",
language = "English",
volume = "146",
pages = "443--447",
journal = "Food Chemistry",
issn = "0308-8146",
publisher = "Elsevier",

}

Antimicrobial activity of antihypertensive food-derived peptides and selected alanine analogues. / McClean, Stephen; Beggs, Louise B; Welch, Rob.

In: Food Chemistry, Vol. 146, 17.01.2014, p. 443-447.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Antimicrobial activity of antihypertensive food-derived peptides and selected alanine analogues

AU - McClean, Stephen

AU - Beggs, Louise B

AU - Welch, Rob

PY - 2014/1/17

Y1 - 2014/1/17

N2 - This study evaluated four food-derived peptides with known antihypertensive activities for antimicrobial activity against pathogenic microorganisms, and assessed structure-function relationships using alanine analogues. The peptides (EVSLNSGYY, barley; PGTAVFK, soybean; TTMPLW, α-casein; VHLPP, α-zein) and the six alanine substitution peptides of PGTAVFK were synthesised, characterised and evaluated for antimicrobial activity using the bacteria, E. coli, S. aureus, and M. luteus and the yeast, C. albicans. The peptides TTMPLW and PGTAVFK inhibited growth of all four microorganisms tested, with activities of a similar order of magnitude to ampicillin and ethanol controls. EVSLNSGYY inhibited the growth of the bacteria, but VHLPP showed no antimicrobial activity. The alanine analogue, PGAAVFK showed the highest overall antimicrobial activity and PGTAVFA showed no activity; overall, the activities of the analogues were consistent with their structures. Some peptides with antihypertensive activity also show antimicrobial activity, suggesting that food-derived peptides may exert beneficia1 effects via a number of mechanisms.

AB - This study evaluated four food-derived peptides with known antihypertensive activities for antimicrobial activity against pathogenic microorganisms, and assessed structure-function relationships using alanine analogues. The peptides (EVSLNSGYY, barley; PGTAVFK, soybean; TTMPLW, α-casein; VHLPP, α-zein) and the six alanine substitution peptides of PGTAVFK were synthesised, characterised and evaluated for antimicrobial activity using the bacteria, E. coli, S. aureus, and M. luteus and the yeast, C. albicans. The peptides TTMPLW and PGTAVFK inhibited growth of all four microorganisms tested, with activities of a similar order of magnitude to ampicillin and ethanol controls. EVSLNSGYY inhibited the growth of the bacteria, but VHLPP showed no antimicrobial activity. The alanine analogue, PGAAVFK showed the highest overall antimicrobial activity and PGTAVFA showed no activity; overall, the activities of the analogues were consistent with their structures. Some peptides with antihypertensive activity also show antimicrobial activity, suggesting that food-derived peptides may exert beneficia1 effects via a number of mechanisms.

U2 - 10.1016/j.foodchem.2013.09.094

DO - 10.1016/j.foodchem.2013.09.094

M3 - Article

VL - 146

SP - 443

EP - 447

JO - Food Chemistry

T2 - Food Chemistry

JF - Food Chemistry

SN - 0308-8146

ER -