Regular paperComparison of the peptide structural requirements for high affinity interaction with bombesin receptors
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Assessment of the bound conformation of bombesin to the BB1 and BB2 receptors
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2020, Journal of Molecular Graphics and ModellingCitation Excerpt :The rest of the structures correspond to partially folded structures, some of them very populated. The presence of helical structures at the C-terminus of the peptide could be associated to the activity of the peptide since bombesin(6–14) is the shortest segment retaining full activity [16,17]. However, there are important structural differences between a α-helix involving residues 6–14 and a partial helix involving a few residues in the middle segment that can be relevant to explain the biological activity of the peptide.
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2018, Applied Surface ScienceInvestigation of bombesin peptide as a targeting ligand for the gastrin releasing peptide (GRP) receptor
2016, Bioorganic and Medicinal ChemistryInsights into bombesin receptors and ligands: Highlighting recent advances
2015, PeptidesCitation Excerpt :A large number of truncated Bn fragments or other synthetic Bn analog are being used for this [241,308,391]. For this reason it is important to remember studies, which show that for the NMBR the minimal COOH terminal, peptide length required for full potency equal to NMB is the COOH terminal decapeptide [179]. For the GRPR the minimal GRPR or Bn COOH terminal fragment demonstrating agonist activity is the COOH-terminal heptapeptide and the minimal COOH fragment required for full affinity equal to Bn or GRP is the COOH-terminal nonapeptide [109,129,179,210].