Binding of the growth factor glycyl‐l‐histidyl‐l‐lysine by heparin

Abstract

Evidence is presented that the growth factor glycyl-histidyl-lysine (GHK) binds to heparin, and the interaction has been characterized by [1H]NMR spectroscopy. 1H chemical shifts indicate that GHK interacts with both the carboxylic acid and the carboxylate forms of heparin. The chemical shift data are consistent with a weak delocalized binding of the triprotonated (ImH+, GlyNH3+, LysNH3+) form of GHK by the carboxylic acid form of heparin. As the pD is increased and the carboxylic acid groups are titrated, chemical shift data indicate that ammonium groups of GHK are hydrogen bonded to heparin carboxylate groups, while the histidyl imidazolium ring occupies the imidazolium-binding site of heparin. Evidence for site-specific binding includes displacement of chemical shift titration curves for heparin to lower pD, increased shielding of specific heparin protons by the imidazolium ring current and displacement of chemical shift titration curves for GHK to higher pD. Specific binding constants were determined for binding of the (ImH+, GlyNH3+), LysNH3+) forms of GHK by the carboxylate form of heparin from chemical shift vs. pD titration data.

Amphiphilic RGD and GHK peptides synergistically enhance liposomal delivery into cancer and endothelial cells

“…9B). These data support the interaction of GHK with heparin in accordance with earlier spectroscopic study 59 and also the idea that GHK-modified liposomes are potentially capable of binding to membrane anionic glycosaminoglycans. Moreover, these results for the first time suggest in situ peptide-modified liposomes as a useful tool to characterize biorelevant interactions of peptide ligands.…”

Biotinylated GHK peptide incorporated collagenous matrix: A novel biomaterial for dermal wound healing in rats

“…The increase in the DNA content, which was parallel to an increase in the protein expression, indicates a process of cell proliferation. High increase of DNA in PIC group may be due to expression of growth factors by BioGHK 31. Most of the growth factors can act as a transcription factor and activates the DNA replication 32…”

“…High increase of DNA in PIC group may be due to expression of growth factors by BioGHK. 31 Most of the growth factors can act as a transcription factor and activates the DNA replication. 32 Wound contraction is a necessary feature of the healing process.…”

Synthesis, structure and stability of novel dimeric peptide‐disulfides

“…We attempted to prepare the monomeric disulfide 4 ( Table 1, Fig. 1 ) by adapting a combination of previously described procedures (2,3). The linear peptide 2 containing free thiol groups was synthesized by a variation of the Boc-protection and HF cleavage techniques of the Merrifield solid-phase peptide synthesis method (6,7).…”

“…Thiol/disulfide interchange reactions provide a means for nature to rearrange the ring size in cyclic peptides. While the synthesis and the stability toward thiol/ disulfide interchange of the 20-membered cyclic peptide disulfides is well studied (2), few reports deal with smaller size rings (3).…”