70396-18-8Relevant articles and documents
CHARACTERIZATION OF A CHIRAL TRIPEPTIDE STATIONARY PHASE FOR THE LIQUID CHROMATOGRAPHIC SEPARATION OF CHIRAL DIPEPTIDES.
Howard,Hsu,Rogers,Nelson
, p. 606 - 610 (1985)
A tripeptide-bonded stationary phase was synthesized by bonding the tripeptide, L-Val-L-Ala-L-Pro, to a reactive silane bonded to silica gel. The retention behavior of several isomeric dipeptides was examined as a function of pH and buffer composition. Although retention behaviors were similar to those reported for the nominally same tripeptide phase prepared in another way, the data indicated that the phases were significantly different. In addition, for the new phase at pH 7. 4, a buffer effect was found in which retentions decreased on going from a phosphate-citrate-chloride (McIlvaine) to phosphate buffer alone, to citrate alone, and to pyrophosphate.
Introducing sequential aza-amino acids units induces repeated β-turns and helical conformations in peptides
Bernadat, Guillaume,Correia, Isabelle,Lequin, Olivier,Lesma, Jacopo,Ongeri, Sandrine,Tonali, Nicolo
supporting information, p. 3452 - 3458 (2020/06/10)
A major current issue in medicinal chemistry is the design of small peptide analogues resistant to proteolysis and able to adopt preferential conformations, while preserving the selectivity and efficiency of natural peptides. Whereas the introduction of one aza-Gly in peptides has proven numerous biological and structural interest, the conformational effect of sequential aza-Gly or aza-amino acids bearing side chains has not been investigated. In this work, experimental NMR and X-ray data together with in silico conformational studies reveal that the introduction of two consecutive aza-amino acids in pseudotripeptides induces the formation of stable hydrogen-bonded β-turn structures. Notably, this stabilization effect relies on the presence of side chains on aza-amino acids, as more flexible conformations are observed with aza-Gly residues. Remarkably, a longer aza/aza/α/aza/aza/α pseudohexapeptide containing substituted aza-amino acids adopts repeated β-turns conformations which interconvert with a fully helical structure mimicking a 310 helix.
The antibody-drug conjugate hemiasterlin derivatives and their pharmaceutically (by machine translation)
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Paragraph 0389; 0433-0434, (2020/12/01)
[Problem] to give one specific target cell cytotoxic, normal cells to the cytotoxic is suppressed, the antibody-drug conjugate medicine hemiasterlin derivatives. (2) Formula [a]:[In the formula, mAb antibody expressed, q is 1 - 8 represents an integer of, h are 1 - 5 represents an integer of, g is an alanine residue (Ala) to represent, g is 1 - 4 represents an integer of, Y is a single bond or a formula (Y-a 1) is represented by the group, Z is formula (Z-a 1), equation (Z-a 2), equation (Z-a 3), formula (Z-a 4), formula (Z-a 5), type (Z-a 6), formula (Za-a 1), equation (Za-in 2), equation (Za-a 3), formula (Za-a 4), formula (Za-a 5), type (Za d 6), formula (Za-a 7), type (Za-in 8), or a group represented by formula (Za-a 10) (Za-a 9) formula a] is expressed by, antibody-drug conjugate or its pharmaceutically acceptable salt containing a drug. [Drawing] no (by machine translation)