90495-99-1Relevant articles and documents
Synthesis of camptothecin-amino acid carbamate linkers
Etienne, Marcus A.,Kostochka, Mikhail,Fuselier, Joseph A.,Coy, David H.
, p. 1727 - 1733 (2012)
A more convenient and facile approach for the synthesis and production of camptothecin-amino acids carbamate linkers, that can be used in the synthesis of bioconjugate peptides JF-10-81, JF-10-71, and other peptide analogs designed to target somatostatin receptors has been described. Springer-Verlag 2011.
Design, development and synthesis of a novel labeled PNA monomer incorporated in DNA-hexamer to act as a hybridization probe by FRET
Shukla, Vibha,Mishra, Satyendra,Watal, Geeta,Misra, Krishna
, p. 121 - 129 (2007/10/03)
A novel PNA monomer with adenine nucleobase and a modified backbone with charged -N+-H and a methylene substituted for 2 bond on the lefthand side sign C=O in the linker arm has been synthesised. This modified PNA monomer is further linked with
Bioactive pseudopeptidic analogues and cyclostereoisomers of osteogenic growth peptide C-terminal pentapeptide, OGP(10-14)
Chen, Yu-Chen,Muhlrad, Andras,Shteyer, Arie,Vidson, Marina,Bab, Itai,Chorev, Michael
, p. 1624 - 1632 (2007/10/03)
The osteogenic growth peptide (OGP) is a key factor in the mechanism of the systemic osteogenic response to local bone marrow injury. When administered in vivo, OGP stimulates osteogenesis and hematopoiesis. The C-terminal pentapeptide OGP(10-14) is the minimal amino acid sequence that retains the full OGP-like activity. Apparently, it is also the physiologic active form of OGP. Residues Tyr10, Phe12, Gly13, and Gly14 of OGP are essential for the OGP(10-14) activity. The present study explored the functional role of the peptide bonds, carboxyl and amino terminal groups, and conformational freedom in OGP(10-14). Transformations replacing the peptide bonds with surrogates such as ψ(CH2NH), ψ(CONMe), and ψ(CH2CH2) demonstrated that amide bonds do not contribute significantly to OGP(10-14) bioactivity. End-to-end cyclization yielded the fully bioactive cyclic pentapeptide c(Tyr-Gly-Phe-Gly-Gly). The retroinverso analogue c(Gly-Gly-phe-Gly-tyr), a cyclostereoisomer of c(Tyr-Gly-Phe-Gly-Gly), is at least as potent as the parent cyclic pentapeptide. The unique structure-activity relations revealed in this study suggest that the spatial presentation of the Tyr and Phe side chains has a major role in the productive interaction of OGP(10-14) and its truncated and conformationally constrained analogues with their cognate cellular target.