Modified β-turns in breast carcinoma-associated MUC1 related peptides

M. J. Scanlon; M. R. Price; S. J B Tendler

Modified β-turns in breast carcinoma-associated MUC1 related peptides

M. J. Scanlon, M. R. Price, S. J B Tendler

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

Abstract

The solution structure of two carcinoma-associated MUC1 core related peptides has been investigated by nuclear magnetic resonance (n.m.r.) spectroscopy. The peptide APDTRPAPG resembles previously studied MUC1 related peptides with a type I β-turn identified in the region PDTR. This portion of the peptide has previously been identified as the binding site for the monoclonal antibodies HMFG-1 and HMFG-2. The peptide where the D has been replaced by its homologue E, which is selectively recognized by the antibody HMFG-1 but not HMFG-2, appears to have a modified turn region. While amide to amide through space connections are observed the results suggest a more open turn structure.

Original language	English
Pages (from-to)	271-273
Number of pages	3
Journal	International Journal of Oncology
Volume	2
Issue number	2
Publication status	Published - 1 Jan 1993
Externally published	Yes

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abstract = "The solution structure of two carcinoma-associated MUC1 core related peptides has been investigated by nuclear magnetic resonance (n.m.r.) spectroscopy. The peptide APDTRPAPG resembles previously studied MUC1 related peptides with a type I β-turn identified in the region PDTR. This portion of the peptide has previously been identified as the binding site for the monoclonal antibodies HMFG-1 and HMFG-2. The peptide where the D has been replaced by its homologue E, which is selectively recognized by the antibody HMFG-1 but not HMFG-2, appears to have a modified turn region. While amide to amide through space connections are observed the results suggest a more open turn structure.",

author = "Scanlon, {M. J.} and Price, {M. R.} and Tendler, {S. J B}",

year = "1993",

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language = "English",

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AU - Scanlon, M. J.

AU - Price, M. R.

AU - Tendler, S. J B

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Y1 - 1993/1/1

N2 - The solution structure of two carcinoma-associated MUC1 core related peptides has been investigated by nuclear magnetic resonance (n.m.r.) spectroscopy. The peptide APDTRPAPG resembles previously studied MUC1 related peptides with a type I β-turn identified in the region PDTR. This portion of the peptide has previously been identified as the binding site for the monoclonal antibodies HMFG-1 and HMFG-2. The peptide where the D has been replaced by its homologue E, which is selectively recognized by the antibody HMFG-1 but not HMFG-2, appears to have a modified turn region. While amide to amide through space connections are observed the results suggest a more open turn structure.

AB - The solution structure of two carcinoma-associated MUC1 core related peptides has been investigated by nuclear magnetic resonance (n.m.r.) spectroscopy. The peptide APDTRPAPG resembles previously studied MUC1 related peptides with a type I β-turn identified in the region PDTR. This portion of the peptide has previously been identified as the binding site for the monoclonal antibodies HMFG-1 and HMFG-2. The peptide where the D has been replaced by its homologue E, which is selectively recognized by the antibody HMFG-1 but not HMFG-2, appears to have a modified turn region. While amide to amide through space connections are observed the results suggest a more open turn structure.

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M3 - Article

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JO - International Journal of Oncology

JF - International Journal of Oncology

SN - 1019-6439

IS - 2

ER -

Modified β-turns in breast carcinoma-associated MUC1 related peptides

Abstract

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