Structure-activity studies of CTL inhibitory peptides derived from HLA class I molecules

Erich J. Schwartz; Jodi Goldberg; Carol Clayberger; Alan M. Krensky; John H. Griffin

doi:10.1016/S0960-894X(96)00576-8

Structure-activity studies of CTL inhibitory peptides derived from HLA class I molecules

Erich J. Schwartz, Jodi Goldberg, Carol Clayberger, Alan M. Krensky, John H. Griffin^*

^*Corresponding author for this work

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

Abstract

A series of dimeric peptides derived from a conserved HLA Class I hexapeptide sequence have been synthesized and tested for their ability to inhibit T cell-mediated lysis and to disrupt membranes. Structure-activity studies of the C-N/N-C dimer show that activity is especially sensitive to substitution of isoleucine residues. The results further define and delimit the basis for activity by HLA-derived peptides.

Original language	English (US)
Pages (from-to)	37-40
Number of pages	4
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	7
Issue number	1
DOIs	https://doi.org/10.1016/S0960-894X(96)00576-8
State	Published - Jan 7 1997

Funding

Acknowledgment. This work was supported by a Program Project Grant from the National Institutes of Health (1P01AI35125, A.M.K., Project Director). E.J.S. was supported in part by a Public Health Services Training Grant (5T32GM07365). J.E.G. was supported by a predoctoral fellowship from the Howard Hughes Medical Institute. Mass spectra were obtained at the UCSF Center for Mass Spectrometry (A.L. Burlingame, Director), supported by the Biomedical Research Technology Program of the NIH NCRR. References and Notes

ASJC Scopus subject areas

Biochemistry
Molecular Medicine
Molecular Biology
Pharmaceutical Science
Drug Discovery
Clinical Biochemistry
Organic Chemistry

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abstract = "A series of dimeric peptides derived from a conserved HLA Class I hexapeptide sequence have been synthesized and tested for their ability to inhibit T cell-mediated lysis and to disrupt membranes. Structure-activity studies of the C-N/N-C dimer show that activity is especially sensitive to substitution of isoleucine residues. The results further define and delimit the basis for activity by HLA-derived peptides.",

author = "Schwartz, {Erich J.} and Jodi Goldberg and Carol Clayberger and Krensky, {Alan M.} and Griffin, {John H.}",

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AU - Schwartz, Erich J.

AU - Goldberg, Jodi

AU - Clayberger, Carol

AU - Krensky, Alan M.

AU - Griffin, John H.

N1 - Funding Information: Acknowledgment. This work was supported by a Program Project Grant from the National Institutes of Health (1P01AI35125, A.M.K., Project Director). E.J.S. was supported in part by a Public Health Services Training Grant (5T32GM07365). J.E.G. was supported by a predoctoral fellowship from the Howard Hughes Medical Institute. Mass spectra were obtained at the UCSF Center for Mass Spectrometry (A.L. Burlingame, Director), supported by the Biomedical Research Technology Program of the NIH NCRR. References and Notes

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AB - A series of dimeric peptides derived from a conserved HLA Class I hexapeptide sequence have been synthesized and tested for their ability to inhibit T cell-mediated lysis and to disrupt membranes. Structure-activity studies of the C-N/N-C dimer show that activity is especially sensitive to substitution of isoleucine residues. The results further define and delimit the basis for activity by HLA-derived peptides.

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Structure-activity studies of CTL inhibitory peptides derived from HLA class I molecules

Abstract

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ASJC Scopus subject areas

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