76587-61-6

Basic information

• Product Name: L-Cysteine, S-(triphenylmethyl)-, 1,1-dimethylethyl ester
• CAS NO: 76587-61-6
• Molecular Formula: C26H29NO2S
• Molecular Weight: 419.588
• Mol File: 76587-61-6.mol
• Article Data: 9

Chemical Properties

• CAS DataBase Reference: L-Cysteine, S-(triphenylmethyl)-, 1,1-dimethylethyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: L-Cysteine, S-(triphenylmethyl)-, 1,1-dimethylethyl ester(76587-61-6)
• EPA Substance Registry System: L-Cysteine, S-(triphenylmethyl)-, 1,1-dimethylethyl ester(76587-61-6)

Safety Data

• Hazardous Substances Data: 76587-61-6(Hazardous Substances Data)

Upstream product

• 71432-55-8 2-tert-butyl-1,3-diisopropylisourea 
• 2799-07-7 S-trityl-L-cysteine 
• 79385-60-7 NS-ditritylcysteine t-butyl ester 
• 540-88-5 acetic acid tert-butyl ester 
• 27686-50-6 N,S-Ditrityl-L-Cystein 
• 302325-60-6 N-[(9-fluorenyl)methoxycarbonyl]-S-(triphenylmethyl)-L-cysteine tert-butyl ester 
• 158009-01-9 tert-Butyl N^α-tert-butoxycarbonyl-L-(S-trityl)cysteinate hydrochloride 
• 103213-32-7 N-(9-fluorenylmethoxycarbonyl)-S-trityl-L-cysteine 
• 76-83-5 trityl chloride 

Downstream Products

• 581799-97-5 N-(1-tert-butoxycarbonyl-2-tritylsulfanyl-ethyl)-3-(9H-fluoren-9-ylmethoxycarbonylamino)-succinamic acid tert-butyl ester 
• 1010440-47-7 N-[(9-fluorenyl)methoxycarbonyl]-L-isoleucyl-S-(triphenylmethyl)-L-cysteine tert-butyl ester 

Relevant articles and documents

MACROCYCLIZATION OF PEPTIDOMIMETICS

The invention provides an improved method of macrocyclization of peptidomimetics, as measured by isolated yields and product distribution, which comprises substitution of one or more of the backbone amide C=O bonds with a turn-inducing motif. The method is general with enhancements seen across a range of ring sizes (e.g. tri-, tetra-, penta- and hexapeptides). Specifically, the invention provides a peptidomimetic macrocycle comprising a carbonyl bioisosteric turn-inducing element having the structure: (I) wherein X is a heteroatom; and wherein R1 to R6 are each independently selected from alkyl, aryl, heteroaryl and H.

Investigation of Cysteine as an Activator of Side-Chain N→S Acyl Transfer and Tail-to-Side-Chain Cyclization

N→S Acyl transfer is a popular method for the postsynthesis production of peptide C α -thioesters for use in native chemical ligation and for the synthesis of head-to-tail cyclic peptides. Meanwhile thioester formation at the side chain of aspartic or glutamic acids, leading to tail-to-side-chain-cyclized species, is less common. Herein we explore the potential for cysteine to function as a latent thioester when appended to the side chain of glutamic acid. Initial insights gained through study of C-terminal β-alanine as a model for the increased chain length were ultimately applied to peptide macrocyclization. Our results emphasize the increased barrier to acyl transfer at the glutamic acid side chain and indicate how a slow reaction, facilitated by cysteine itself, may be accelerated by fine-tuning of the stereoelectronic environment..

Carbohydrate-based VEGF inhibitors

Cyclic peptide-carbohydrates (compounds 1a-c, 2, 33, 34) were designed and synthesized to act as mimetics of loop 2 of the proangiogenic molecule vascular endothelial growth factor D (VEGF-D). The mimetics were designed to inhibit dimerization of the receptors (VEGFR-2 and VEGFR-3) by VEGF-D, and thus have the potential to inhibit angiogenesis. To this end, in the previously described cyclic octapeptide CNEESLIC and the cyclic nonapeptide CGNEESLIC inhibitors derived from VEGF-D loop 2, the NEES tetrapeptide residue was replaced by a carbohydrate scaffold having the amino acid side chain mimics in positions proposed by modeling studies. Attachment of the additional amino acids using the Fmoc technology, then formation of the cyclic disulfides, and finally total deprotection afforded the target molecules of which 2 and 34 showed an ability to inhibit the biological activity of VEGF-D through VEGFR-2 in cell-based assays, albeit at high mimetic concentration. Wiley-VCH Verlag GmbH & Co. KGaA, 2007.