Peptides as active probes

Undén, Anders; Bartfai, T.

doi:10.1007/978-3-0348-9061-8_11

Cited by 3 publications

(3 citation statements)

References 67 publications

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“…Specific structural features appear to be important for the capacity of C-peptide to bind to cell membranes and to elicit biological effects, as is the case for other peptide hormones (24). FCS studies established that C-peptide at physiological, low nanomolar, concentrations binds to human renal tubular cell membranes, and that bound C-peptide is displaced by the C-terminal pentapeptide segment (19).…”

Section: Discussionmentioning

confidence: 97%

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C-Peptide Binding to Human Cell Membranes: Importance of Glu27

Pramanik

Ekberg

Zhong

et al. 2001

Biochemical and Biophysical Research Communications

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Section: Discussionmentioning

confidence: 97%

“…Peptide hormones often carry a limited number of functional groups that are essential for receptor binding (24). It would then seem as if C-peptide binding to cellular targets is mediated by its C-terminal pentapeptide segment, with Glu27 being crucial for this interaction.…”

Section: Discussionmentioning

confidence: 99%

C-Peptide Binding to Human Cell Membranes: Importance of Glu27

Pramanik

Ekberg

Zhong

et al. 2001

Biochemical and Biophysical Research Communications

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“…Synthetic peptides are in principle good candidates for the development of new drugs and diagnostic tools, because of their favourable chemical and physical properties such as low toxicity and easy handling and storage [1]. Methods for their largescale synthesis are well known and several steps are fully automated [2].…”

Section: Introductionmentioning

confidence: 99%

NMR studies on Ni(II) induced cyclization of a histidine‐tagged peptide

Spiga

Bernini

Scarselli

et al. 2002

Journal of Peptide Science

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A linear decapeptide, HGASYQDLGH, was synthesized and used as a model to evaluate the effect of nickel addition upon non-covalent backbone cyclization. The NMR data, obtained for the peptide in the presence of the metal ion, support the existence of predominant folded structures in solution, where the two His residues are maintained close to each other. These results suggest that insertion of even a single His residue at each peptide terminus can be used efficiently to reduce peptide flexibility without any backbone modification.

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Design of peptides, proteins, and peptidomimetics in chi space

et al. 1997

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Peptide and protein biological activities depend on their three dimensionals structures in the free state and when interacting with their receptors/acceptors. The backbone conformations such as α‐helix, β‐sheet, β‐turn, and so forth provide critical templates for the three‐dimensional structure, but the overall shape and intrinsic stereoelectronic properties of the peptide or protein important for molecular recognition, signal transduction, enzymatic specificity, immunomodulation, and other biological effects depend on arrangement of the side chain groups in three‐dimensional chi space (their χ1, χ2, etc. torsional angles) In this paper we explore approaches to the de novo design of polypeptides and peptidomimetics with biased or specific conformational/topographical properties in chi space. We consider computational and experimental methods that can be used to examine the effects of specific structural modifications in constraining side chain groups of amino acid residues and their similarities in chi space to the natural amino acids to evaluate what sort of mimetics are likely to minic normal amino acids. We then examine some of the asymmetric synthetic methods that are being developed to obtain the amino acid mimetics. Finally, we consider selected examples in the literature where these specialized amino acids have been incorporated in biologically active peptides and the specific insights they have provided regarding the topographical requirements for bioactive peptide potency, selectivity, and other biochemical and pharmacological properties. Constraints in chi space show great promise as useful tools in peptide, protein, and peptidomimetic de novo design of structures and pharmacophores with specific stereostructural, biochemical and biological properties. © 1997 John Wiley & Sons, Inc. Biopoly 43: 219–266, 1997

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Peptides as active probes

Cited by 3 publications

References 67 publications

C-Peptide Binding to Human Cell Membranes: Importance of Glu27

C-Peptide Binding to Human Cell Membranes: Importance of Glu27

NMR studies on Ni(II) induced cyclization of a histidine‐tagged peptide

Design of peptides, proteins, and peptidomimetics in chi space

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