Two amphiphilic, synthetic peptides display strong emulsification properties

K. B. Carey; S. M. Kelly; N. C. Price; D. J. O'Sullivan; D. Sheehan

doi:10.1016/0308-8146(94)90097-3

Two amphiphilic, synthetic peptides display strong emulsification properties

K. B. Carey
, S. M. Kelly
, N. C. Price
, D. J. O'Sullivan
, D. Sheehan

Chemistry

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

6 Scopus citations

Abstract

Two amphiphilic peptides with the following sequences were designed and synthesised: peptide 1, TFLQDLKEKVQQLTEALK; petide 2, TVSQLQEYWT-TLLSQIKTLLQQIKTS. The emulsification properties of these peptides were tested in an oil-water two-phase system and were found to be significantly greater than those of mellitin. Circular dichroism measurement were used to characterise the secondary structure of the peptides. In aqueous buffer, they adopted c. 50% beta sheet conformation.

Original language	British English
Pages (from-to)	83-85
Number of pages	3
Journal	Food Chemistry
Volume	50
Issue number	1
DOIs	https://doi.org/10.1016/0308-8146(94)90097-3
State	Published - 1994

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title = "Two amphiphilic, synthetic peptides display strong emulsification properties",

abstract = "Two amphiphilic peptides with the following sequences were designed and synthesised: peptide 1, TFLQDLKEKVQQLTEALK; petide 2, TVSQLQEYWT-TLLSQIKTLLQQIKTS. The emulsification properties of these peptides were tested in an oil-water two-phase system and were found to be significantly greater than those of mellitin. Circular dichroism measurement were used to characterise the secondary structure of the peptides. In aqueous buffer, they adopted c. 50\% beta sheet conformation.",

author = "Carey, \{K. B.\} and Kelly, \{S. M.\} and Price, \{N. C.\} and O'Sullivan, \{D. J.\} and D. Sheehan",

year = "1994",

doi = "10.1016/0308-8146(94)90097-3",

language = "British English",

volume = "50",

pages = "83--85",

journal = "Food Chemistry",

issn = "0308-8146",

publisher = "Elsevier Ltd",

number = "1",

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T1 - Two amphiphilic, synthetic peptides display strong emulsification properties

AU - Carey, K. B.

AU - Kelly, S. M.

AU - Price, N. C.

AU - O'Sullivan, D. J.

AU - Sheehan, D.

PY - 1994

Y1 - 1994

N2 - Two amphiphilic peptides with the following sequences were designed and synthesised: peptide 1, TFLQDLKEKVQQLTEALK; petide 2, TVSQLQEYWT-TLLSQIKTLLQQIKTS. The emulsification properties of these peptides were tested in an oil-water two-phase system and were found to be significantly greater than those of mellitin. Circular dichroism measurement were used to characterise the secondary structure of the peptides. In aqueous buffer, they adopted c. 50% beta sheet conformation.

AB - Two amphiphilic peptides with the following sequences were designed and synthesised: peptide 1, TFLQDLKEKVQQLTEALK; petide 2, TVSQLQEYWT-TLLSQIKTLLQQIKTS. The emulsification properties of these peptides were tested in an oil-water two-phase system and were found to be significantly greater than those of mellitin. Circular dichroism measurement were used to characterise the secondary structure of the peptides. In aqueous buffer, they adopted c. 50% beta sheet conformation.

UR - https://www.scopus.com/pages/publications/0028355472

U2 - 10.1016/0308-8146(94)90097-3

DO - 10.1016/0308-8146(94)90097-3

M3 - Article

AN - SCOPUS:0028355472

SN - 0308-8146

VL - 50

SP - 83

EP - 85

JO - Food Chemistry

JF - Food Chemistry

IS - 1

ER -

Two amphiphilic, synthetic peptides display strong emulsification properties

Abstract

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