ChemInform Abstract: CONFORMATIONAL PREFERENCES OF THE BRIDGING GROUPS OF CYCLO-L-CYSTINE AND THE ACTIVE FRAGMENTS OF EPIPOLYTHIODIKETOPIPERAZINE ANTIBIOTICS

A. R. GREGORY; M. PRZYBYLSKA

doi:10.1002/chin.197821068

ChemInform Abstract: CONFORMATIONAL PREFERENCES OF THE BRIDGING GROUPS OF CYCLO-L-CYSTINE AND THE ACTIVE FRAGMENTS OF EPIPOLYTHIODIKETOPIPERAZINE ANTIBIOTICS

Chemischer Informationsdienst ◽

10.1002/chin.197821068 ◽

1978 ◽

Vol 9 (21) ◽

Author(s):

A. R. GREGORY ◽

M. PRZYBYLSKA

Keyword(s):

Conformational Preferences ◽

Active Fragments ◽

Bridging Groups

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Conformational preferences of the bridging groups of cyclo-L-cystine and the active fragments of epipolythiodiketopiperazine antibiotics

Journal of the American Chemical Society ◽

10.1021/ja00471a048 ◽

1978 ◽

Vol 100 (3) ◽

pp. 943-949 ◽

Cited By ~ 6

Author(s):

Allan R. Gregory ◽

Maria Przybylska

Keyword(s):

Conformational Preferences ◽

Active Fragments ◽

Bridging Groups

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Permeability Enhancing and Chemotactic Activities of Lower Molecular Weight Degradation Products of Human Fibrinogen

Thrombosis and Haemostasis ◽

10.1055/s-0038-1650136 ◽

1981 ◽

Vol 45 (01) ◽

pp. 090-094 ◽

Cited By ~ 52

Author(s):

Katsuo Sueishi ◽

Shigeru Nanno ◽

Kenzo Tanaka

Keyword(s):

Molecular Weight ◽

Degradation Products ◽

Electron Microscopic Observation ◽

Chemotactic Activity ◽

Lower Molecular Weight ◽

Electron Microscopic ◽

Human Fibrinogen ◽

Rabbit Skin ◽

Molecular Weights ◽

Active Fragments

SummaryFibrinogen degradation products were investigated for leukocyte chemotactic activity and for enhancement of vascular permeability. Both activities increased progressively with plasmin digestion of fibrinogen. Active fragments were partially purified from 24 hr-plasmin digests. Molecular weights of the permeability increasing and chemotactic activity fractions were 25,000-15,000 and 25,000 respectively. Both fractions had much higher activities than the fragment X, Y, D or E. Electron microscopic observation of the small blood vessels in rabbit skin correlated increased permeability with the formation of characteristic gaps between adjoining endothelial cells and their contraction.These findings suggest that lower molecular weight degradation products of fibrinogen may be influential in contributing to granulocytic infiltration and enhanced permeability in lesions characterized by deposits of fibrin and/or fibrinogen.

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CONFORMER-SPECIFIC IR SPECTROSCOPY OF LASER-DESORBED SULFONAMIDE DRUGS: TAUTOMERIC AND CONFORMATIONAL PREFERENCES OF SULFANILAMIDE AND ITS DERIVATIVES

Proceedings of the 72nd International Symposium on Molecular Spectroscopy ◽

10.15278/isms.2017.wc10 ◽

2017 ◽

Author(s):

Thomas Uhlemann ◽

Christian Müller ◽

Sebastian Seidel

Keyword(s):

Ir Spectroscopy ◽

Conformational Preferences

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EFFECT OF INTRAMOLECULAR DISPERSION INTERACTIONS ON THE CONFORMATIONAL PREFERENCES OF MONOTERPENOIDS

Proceedings of the 72nd International Symposium on Molecular Spectroscopy ◽

10.15278/isms.2017.wc03 ◽

2017 ◽

Author(s):

Donatella Loru ◽

M. Sanz ◽

Jackson Tang ◽

Andreia Santos ◽

Annalisa Vigorito

Keyword(s):

Dispersion Interactions ◽

Conformational Preferences

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Faculty Opinions recommendation of Contact order dependent protein folding rates: kinetic consequences of a cooperative interplay between favorable nonlocal interactions and local conformational preferences.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1015714.197907 ◽

2003 ◽

Author(s):

Eaton E Lattman

Keyword(s):

Protein Folding ◽

Nonlocal Interactions ◽

Folding Rates ◽

Contact Order ◽

Conformational Preferences ◽

Dependent Protein

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NMR spectroscopy in the conformational analysis of peptides: an overview

Current Medicinal Chemistry ◽

10.2174/0929867327666200702131032 ◽

2020 ◽

Vol 27 ◽

Author(s):

Marian Vincenzi ◽

Flavia Anna Mercurio ◽

Marilisa Leone

Keyword(s):

Nmr Spectroscopy ◽

Protein Interactions ◽

3D Structure ◽

Theoretical Background ◽

Triple Resonance ◽

Protein Protein Interactions ◽

Nmr Studies ◽

Conformational Preferences ◽

Dynamic Perspective ◽

Nmr Methods

Background: NMR spectroscopy is one of the most powerful tools to study the structure and interaction properties of peptides and proteins from a dynamic perspective. Knowing the bioactive conformations of peptides is crucial in the drug discovery field to design more efficient analogue ligands and inhibitors of protein-protein interactions targeting therapeutically relevant systems. Objective: This review provides a toolkit to investigate peptide conformational properties by NMR. Methods: Articles cited herein, related to NMR studies of peptides and proteins were mainly searched through Pubmed and the web. More recent and old books on NMR spectroscopy written by eminent scientists in the field were consulted as well. Results: The review is mainly focused on NMR tools to gain the 3D structure of small unlabeled peptides. It is more application-oriented as it is beyond its goal to deliver a profound theoretical background. However, the basic principles of 2D homonuclear and heteronuclear experiments are briefly described. Protocols to obtain isotopically labeled peptides and principal triple resonance experiments needed to study them, are discussed as well. Conclusion: NMR is a leading technique in the study of conformational preferences of small flexible peptides whose structure can be often only described by an ensemble of conformations. Although NMR studies of peptides can be easily and fast performed by canonical protocols established a few decades ago, more recently we have assisted to tremendous improvements of NMR spectroscopy to investigate instead large systems and overcome its molecular weight limit.

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