Quantitative interactions between cryptdin-4 amino terminal variants and membranes

Donald P. Satchell; Tanya Sheynis; Sofiya Kolusheva; Jason Cummings; T. Kyle Vanderlick; Raz Jelinek; Michael E. Selsted; Andre J. Ouellette

doi:10.1016/j.peptides.2003.08.020

Quantitative interactions between cryptdin-4 amino terminal variants and membranes

Donald P. Satchell, Tanya Sheynis, Sofiya Kolusheva, Jason Cummings, T. Kyle Vanderlick, Raz Jelinek, Michael E. Selsted, Andre J. Ouellette

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

50 Scopus citations

Abstract

Paneth cells secrete α-defensins into the lumen from the base of small intestinal crypts, and cryptdin-4 (Crp4) is the most potent mouse α-defensin in vitro. Purified recombinant Crp4 and Crp4 variants with (des-Gly)-, (Gly1Val)-, (Gly1Asp)-, and (Gly1Arg)-substitutions were all bactericidal with Crp4 and (Gly1Arg)-Crp4 being slightly more active than other variants. Bactericidal activities correlated directly with permeabilization of live Escherichia coli, with equilibrium binding to E. coli membrane phospholipid bilayers and vesicles, and with induced graded fluorophore leakage from phospholipid vesicles. The Crp4 peptide N-terminus affects bactericidal activity modestly, apparently by influencing peptide binding to phospholipid bilayers and subsequent permeabilization of target cell membranes.

Original language	English
Pages (from-to)	1795-1805
Number of pages	11
Journal	Peptides
Volume	24
Issue number	11
DOIs	https://doi.org/10.1016/j.peptides.2003.08.020
State	Published - 1 Jan 2003

Keywords

Innate immunity
Matrix-assisted laser desorption time-of-flight mass spectrometry
Paneth cells
Polymerase chain reaction
Recombinant peptide expression
Reverse-phase high performance liquid chromatography
Surface plasmon resonance
α-Defensin

ASJC Scopus subject areas

Biochemistry
Physiology
Endocrinology
Cellular and Molecular Neuroscience

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.peptides.2003.08.020

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title = "Quantitative interactions between cryptdin-4 amino terminal variants and membranes",

abstract = "Paneth cells secrete α-defensins into the lumen from the base of small intestinal crypts, and cryptdin-4 (Crp4) is the most potent mouse α-defensin in vitro. Purified recombinant Crp4 and Crp4 variants with (des-Gly)-, (Gly1Val)-, (Gly1Asp)-, and (Gly1Arg)-substitutions were all bactericidal with Crp4 and (Gly1Arg)-Crp4 being slightly more active than other variants. Bactericidal activities correlated directly with permeabilization of live Escherichia coli, with equilibrium binding to E. coli membrane phospholipid bilayers and vesicles, and with induced graded fluorophore leakage from phospholipid vesicles. The Crp4 peptide N-terminus affects bactericidal activity modestly, apparently by influencing peptide binding to phospholipid bilayers and subsequent permeabilization of target cell membranes.",

keywords = "Innate immunity, Matrix-assisted laser desorption time-of-flight mass spectrometry, Paneth cells, Polymerase chain reaction, Recombinant peptide expression, Reverse-phase high performance liquid chromatography, Surface plasmon resonance, α-Defensin",

author = "Satchell, {Donald P.} and Tanya Sheynis and Sofiya Kolusheva and Jason Cummings and Vanderlick, {T. Kyle} and Raz Jelinek and Selsted, {Michael E.} and Ouellette, {Andre J.}",

note = "Funding Information: Supported by NIH grants DK10184 (D.P.S.), AI22931 (M.E.S.), and DK44632 (A.J.O.) and the United States-Israel Binational Science Foundation (A.J.O., R.J.). R.J. is a member of the Ilse Katz Center for Meso- and Nanoscience and Technology, and J.E.C. acknowledges support from an NSF Fellowship. We thank Tim Cole, Vungie Hoang, and Khoa Nguyen for excellent technical assistance. Surface plasmon resonance studies were performed in the UCI Optical Biology Core Facility.",

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doi = "10.1016/j.peptides.2003.08.020",

language = "English",

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pages = "1795--1805",

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T1 - Quantitative interactions between cryptdin-4 amino terminal variants and membranes

AU - Satchell, Donald P.

AU - Sheynis, Tanya

AU - Kolusheva, Sofiya

AU - Cummings, Jason

AU - Vanderlick, T. Kyle

AU - Jelinek, Raz

AU - Selsted, Michael E.

AU - Ouellette, Andre J.

N1 - Funding Information: Supported by NIH grants DK10184 (D.P.S.), AI22931 (M.E.S.), and DK44632 (A.J.O.) and the United States-Israel Binational Science Foundation (A.J.O., R.J.). R.J. is a member of the Ilse Katz Center for Meso- and Nanoscience and Technology, and J.E.C. acknowledges support from an NSF Fellowship. We thank Tim Cole, Vungie Hoang, and Khoa Nguyen for excellent technical assistance. Surface plasmon resonance studies were performed in the UCI Optical Biology Core Facility.

PY - 2003/1/1

Y1 - 2003/1/1

N2 - Paneth cells secrete α-defensins into the lumen from the base of small intestinal crypts, and cryptdin-4 (Crp4) is the most potent mouse α-defensin in vitro. Purified recombinant Crp4 and Crp4 variants with (des-Gly)-, (Gly1Val)-, (Gly1Asp)-, and (Gly1Arg)-substitutions were all bactericidal with Crp4 and (Gly1Arg)-Crp4 being slightly more active than other variants. Bactericidal activities correlated directly with permeabilization of live Escherichia coli, with equilibrium binding to E. coli membrane phospholipid bilayers and vesicles, and with induced graded fluorophore leakage from phospholipid vesicles. The Crp4 peptide N-terminus affects bactericidal activity modestly, apparently by influencing peptide binding to phospholipid bilayers and subsequent permeabilization of target cell membranes.

AB - Paneth cells secrete α-defensins into the lumen from the base of small intestinal crypts, and cryptdin-4 (Crp4) is the most potent mouse α-defensin in vitro. Purified recombinant Crp4 and Crp4 variants with (des-Gly)-, (Gly1Val)-, (Gly1Asp)-, and (Gly1Arg)-substitutions were all bactericidal with Crp4 and (Gly1Arg)-Crp4 being slightly more active than other variants. Bactericidal activities correlated directly with permeabilization of live Escherichia coli, with equilibrium binding to E. coli membrane phospholipid bilayers and vesicles, and with induced graded fluorophore leakage from phospholipid vesicles. The Crp4 peptide N-terminus affects bactericidal activity modestly, apparently by influencing peptide binding to phospholipid bilayers and subsequent permeabilization of target cell membranes.

KW - Innate immunity

KW - Matrix-assisted laser desorption time-of-flight mass spectrometry

KW - Paneth cells

KW - Polymerase chain reaction

KW - Recombinant peptide expression

KW - Reverse-phase high performance liquid chromatography

KW - Surface plasmon resonance

KW - α-Defensin

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DO - 10.1016/j.peptides.2003.08.020

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JO - Peptides

JF - Peptides

IS - 11

ER -

Quantitative interactions between cryptdin-4 amino terminal variants and membranes

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

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