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Linear and cyclic N-terminal galanin fragments and analogs as ligands at the hypothalamic galanin receptor

Academic Article
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Overview

authors

  • Land, T.
  • Langel, Ülo
  • Low, M.
  • Berthold, M.
  • Unden, A.
  • Bartfai, Tamas

publication date

  • September 1991

journal

  • International Journal of Peptide and Protein Research  Journal

abstract

  • The neuropeptide galanin (1-29) binds with high affinity to hypothalamic receptors (KD approximately 0.9 nM) and regulates feeding behavior. The N-terminal fragments (1-16), (1-16)NH2 are high affinity (KD approximately 6 nM) full agonists in vivo and in vitro. L-Ala substitutions show that amino acid residues Gly1, Trp2, Asn5, Tyr9, and Gly12 are important for the high affinity binding of galanin (1-16). Shortening the fragment (1-16) to galanin (1-7) causes a gradual drop of affinity: galanin (1-15), (1-14), and (1-13) have submicromolar KD values and galanin (1-12) has KD approximately 3 microM. Cyclic analogs of galanin (1-12) of different ring size were synthesized by condensing Gly1 and Gly12 without or with spacer groups. These analogs, independent of ring size, had a lower affinity than the linear galanin (1-12). Derivatization of the N-terminus of galanin (1-29), (1-16), and (1-12) all resulted in a large drop of affinity for the receptors, suggesting again the importance of the free N-terminal Gly.

subject areas

  • Alanine
  • Amino Acid Sequence
  • Amino Acids
  • Animals
  • Binding Sites
  • Feeding Behavior
  • Galanin
  • Hypothalamus
  • Male
  • Molecular Sequence Data
  • Neuropeptides
  • Peptides
  • Peptides, Cyclic
  • Rats
  • Receptors, Galanin
  • Receptors, Gastrointestinal Hormone
  • Sequence Homology, Nucleic Acid
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Research

keywords

  • GALANIN FRAGMENTS AND ANALOGS
  • RECEPTOR BINDING
  • SOLID PHASE SYNTHESIS
  • STRUCTURE-ACTIVITY RELATIONSHIP
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Identity

International Standard Serial Number (ISSN)

  • 0367-8377

Digital Object Identifier (DOI)

  • 10.1111/j.1399-3011.1991.tb01438.x

PubMed ID

  • 1722197
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Additional Document Info

start page

  • 267

end page

  • 272

volume

  • 38

issue

  • 3

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