A GGCT fluorogenic probe: design, synthesis and application to cancer-related cells

2015 ◽  
Vol 13 (11) ◽  
pp. 3182-3185 ◽  
Author(s):  
Taku Yoshiya ◽  
Hiromi Ii ◽  
Shugo Tsuda ◽  
Susumu Kageyama ◽  
Tatsuhiro Yoshiki ◽  
...  
Keyword(s):  
Amino Acids ◽  
Probe Design ◽  
Design Synthesis ◽  
Fluorogenic Probe

Cancer-related γ-glutamyl cyclotransferase (GGCT) specifically decomposes γ-glutamyl amino acids. Here we report a novel GGCT fluorogenic probe “LISA-101”.

Antiovulatory Potency and Conformation of an Antagonist of the Luteinizing Hormone-Releasing Hormone Having Six D-Amino Acids

1982 ◽  
Vol 37 (7) ◽  
pp. 872-876 ◽  
Author(s):  
Karl Folkers ◽  
Cyril Y. Bowers ◽  
Frank Momany ◽  
Klaus J. Friebel ◽  
Teresa Kubiak ◽  
...  
Keyword(s):  
Amino Acids ◽  
Luteinizing Hormone ◽  
Conformational Structure ◽  
Design Synthesis ◽  
Luteinizing Hormone Releasing Hormone ◽  
Energy Calculations ◽  
Releasing Hormone ◽  
Routes Of Administration ◽  
Antiovulatory Activity

Abstract [N-Ac-Thr 1 ,D-Phe 2,D-Trp 3,6]-LHRH was the model antagonist of LHRH, which was the basis for tho design, synthesis and bioassay of seven peptides having four, five and six D-amino acids, which resulted from three single, three double, and one triple introductions of D-amino acids in positions 4, 5 and 8 of the model. Only the analog with six D-amino acids, [N-Ac-Thr 1,D-Phe 2 ,D-Trp 3,D-Ser 4, D-Tyr 5 ,D-Trp 6 ,D-Arg 8]-LHRH, had antiovulatory activity which was higher than that of the model antagonist, i.e., 70% antiovulatory activity at 25 μg/rat compared with 50% activity at 50 μg/rat, respectively. Empirical energy calculations gave a conformational structure for [N-Ac-Thr 1,D-Phe 2,D-Trp 3, D-Ser 4,D-Tyr 5,D-Arg 6,D-Arg 8]-LHRH which is similar to that calculated for previous potent antagonists. These results are a basis of new designs of antagonists having D-sub-stituents in up to ten positions toward effective inhibitors of ovulation by the parenteral and oral routes of administration.

Design, Synthesis, Conformational Analysis and Application of Azabicycloalkane Amino Acids as Constrained Dipeptide Mimics

ChemInform ◽  
2004 ◽  
Vol 35 (40) ◽  
Author(s):  
Laura Belvisi ◽  
Lino Colombo ◽  
Leonardo Manzoni ◽  
Donatella Potenza ◽  
Carlo Scolastico
Keyword(s):  
Amino Acids ◽  
Conformational Analysis ◽  
Design Synthesis

scholarly journals Abc Amino Acids: Design, Synthesis, and Properties of New Photoelastic Amino Acids

ChemInform ◽  
2007 ◽  
Vol 38 (7) ◽  
Author(s):  
Robert F. Standaert ◽  
Seung Bum Park
Keyword(s):  
Amino Acids ◽  
Design Synthesis

scholarly journals Labeling Preferences of Diazirines with Protein Biomolecules

2020 ◽  
Author(s):  
Alexander West ◽  
Giovanni Muncipinto ◽  
Hung-Yi Wu ◽  
Andrew Huang ◽  
Matthew T. Labenski ◽  
...  
Keyword(s):  
Amino Acids ◽  
Systematic Evaluation ◽  
Probe Design ◽  
Dependent Manner ◽  
Membrane Proteome ◽  
Non Covalent Interactions ◽  
Acidic Proteins ◽  
Cell Proteome ◽  
Covalent Interactions ◽  
Net Positive Charge

<p>Diazirines are widely used in photoaffinity labeling (PAL) to trap non-covalent interactions with biomolecules. However, design and interpretation of PAL experiments is challenging without a molecular understanding of the reactivity of diazirines with protein biomolecules. Here, we report a systematic evaluation of the labeling preferences of alkyl and aryl diazirines with individual amino acids, single proteins, and in the whole cell proteome. We find that aryl-fluorodiazirines react primarily through a carbene intermediate, while alkyl diazirines generate a reactive alkyl diazo intermediate on route to the carbene. The generation of a reactive diazo intermediate leads to preferential labeling of acidic amino acids in a pH-dependent manner. From a survey of 32 alkyl diazirine probes, we use this reactivity profile to rationalize why these probes preferentially enrich highly acidic proteins or those embedded in membranes and why probes with a net positive-charge tend to produce higher labeling yields. These results indicate that alkyl diazirines are an especially effective chemistry for surveying the membrane proteome, and will facilitate probe design and interpretation of biomolecular labeling experiments with diazirines.<b></b></p>

scholarly journals Design, Synthesis, and Biological Evaluation of Beauveriolide Analogues Bearing Photoreactive Amino Acids

2016 ◽  
Vol 64 (7) ◽  
pp. 754-765 ◽  
Author(s):  
Yuichi Masuda ◽  
Kazumasa Aoyama ◽  
Masahito Yoshida ◽  
Keisuke Kobayashi ◽  
Taichi Ohshiro ◽  
...  
Keyword(s):  
Amino Acids ◽  
Biological Evaluation ◽  
Design Synthesis ◽  
Synthesis And Biological Evaluation
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