Synthetic peptides corresponding to α-lactalbumin and β-lactoglobulin sequences with angiotensin-i-converting enzyme inhibitory activity

Margaret M. Mullally; Hans Meisel; Richard J. Fitzgerald

Synthetic peptides corresponding to α-lactalbumin and β-lactoglobulin sequences with angiotensin-i-converting enzyme inhibitory activity

Margaret M. Mullally, Hans Meisel, Richard J. Fitzgerald

Research output: Contribution to journal › Article › peer-review

Abstract

Novel angiotensin-l-converting enzyme (ACE) inhibitory activities were detected in synthetic peptides corresponding to sequences of β-lactoglobulin and α-lactalbumin and which are known to possess opioid activity. Using hippuryl-histidyl-leucine as substrate, the tetrapeptides β-lactorphin (Tyr-Leu-Leu-Phe), alactorphin (Tyr-Gly-Leu-Phe) and β-lactotensin (HisIle-Arg-Leu) were shown to have ICso values of 171.8, 733.3 and 1153.2 JAM, respectively. Related dipeptides also inhibited ACE, with Tyr-Leu being the most potent, having an ICso value of 122.1 \M.

Original language	English
Pages (from-to)	259-260
Number of pages	2
Journal	Biological Chemistry Hoppe-Seyler
Volume	377
Issue number	4
Publication status	Published - 1996
Externally published	Yes

Keywords

IC50
Multifunctional bioactivity
Nutraceutical
Opioid peptides

Cite this

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title = "Synthetic peptides corresponding to α-lactalbumin and β-lactoglobulin sequences with angiotensin-i-converting enzyme inhibitory activity",

abstract = "Novel angiotensin-l-converting enzyme (ACE) inhibitory activities were detected in synthetic peptides corresponding to sequences of β-lactoglobulin and α-lactalbumin and which are known to possess opioid activity. Using hippuryl-histidyl-leucine as substrate, the tetrapeptides β-lactorphin (Tyr-Leu-Leu-Phe), alactorphin (Tyr-Gly-Leu-Phe) and β-lactotensin (HisIle-Arg-Leu) were shown to have ICso values of 171.8, 733.3 and 1153.2 JAM, respectively. Related dipeptides also inhibited ACE, with Tyr-Leu being the most potent, having an ICso value of 122.1 \textbackslash{}M.",

keywords = "IC50, Multifunctional bioactivity, Nutraceutical, Opioid peptides",

author = "Mullally, \{Margaret M.\} and Hans Meisel and Fitzgerald, \{Richard J.\}",

year = "1996",

language = "English",

volume = "377",

pages = "259--260",

journal = "Biological Chemistry Hoppe-Seyler",

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T1 - Synthetic peptides corresponding to α-lactalbumin and β-lactoglobulin sequences with angiotensin-i-converting enzyme inhibitory activity

AU - Mullally, Margaret M.

AU - Meisel, Hans

AU - Fitzgerald, Richard J.

PY - 1996

Y1 - 1996

N2 - Novel angiotensin-l-converting enzyme (ACE) inhibitory activities were detected in synthetic peptides corresponding to sequences of β-lactoglobulin and α-lactalbumin and which are known to possess opioid activity. Using hippuryl-histidyl-leucine as substrate, the tetrapeptides β-lactorphin (Tyr-Leu-Leu-Phe), alactorphin (Tyr-Gly-Leu-Phe) and β-lactotensin (HisIle-Arg-Leu) were shown to have ICso values of 171.8, 733.3 and 1153.2 JAM, respectively. Related dipeptides also inhibited ACE, with Tyr-Leu being the most potent, having an ICso value of 122.1 \M.

AB - Novel angiotensin-l-converting enzyme (ACE) inhibitory activities were detected in synthetic peptides corresponding to sequences of β-lactoglobulin and α-lactalbumin and which are known to possess opioid activity. Using hippuryl-histidyl-leucine as substrate, the tetrapeptides β-lactorphin (Tyr-Leu-Leu-Phe), alactorphin (Tyr-Gly-Leu-Phe) and β-lactotensin (HisIle-Arg-Leu) were shown to have ICso values of 171.8, 733.3 and 1153.2 JAM, respectively. Related dipeptides also inhibited ACE, with Tyr-Leu being the most potent, having an ICso value of 122.1 \M.

KW - IC50

KW - Multifunctional bioactivity

KW - Nutraceutical

KW - Opioid peptides

UR - https://www.scopus.com/pages/publications/0029937138

M3 - Article

C2 - 8737991

AN - SCOPUS:0029937138

SN - 0177-3593

VL - 377

SP - 259

EP - 260

JO - Biological Chemistry Hoppe-Seyler

JF - Biological Chemistry Hoppe-Seyler

IS - 4

ER -

Synthetic peptides corresponding to α-lactalbumin and β-lactoglobulin sequences with angiotensin-i-converting enzyme inhibitory activity

Abstract

Keywords

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