86895-14-9Relevant articles and documents
Site-selective chemical cleavage of peptide bonds
Elashal, Hader E.,Raj, Monika
supporting information, p. 6304 - 6307 (2016/05/24)
Site-selective cleavage of extremely unreactive peptide bonds is a very important chemical modification that provides invaluable information regarding protein sequence, and it acts as a modulator of protein structure and function for therapeutic applications. For controlled and selective cleavage, a daunting task, chemical reagents must selectively recognize or bind to one or more amino acid residues in the peptide chain and selectively cleave a peptide bond. Building on this principle, we have developed an approach that utilizes a chemical reagent to selectively modify the serine residue in a peptide chain and leads to the cleavage of a peptide backbone at the N-terminus of the serine residue. After cleavage, modified residues can be converted back to the original fragments. This method exhibits broad substrate scope and selectively cleaves various bioactive peptides with post-translational modifications (e.g. N-acetylation and -methylation) and mutations (d- and β-amino acids), which are a known cause of age related diseases.
Characterization of Nα-Fmoc-protected dipeptide isomers by electrospray ionization tandem mass spectrometry (ESI-MSn): Effect of protecting group on fragmentation of dipeptides
Ramesh,Raju,Srinivas,Sureshbabu,Vishwanatha,Hemantha
experimental part, p. 1949 - 1958 (2012/05/20)
A series of positional isomeric pairs of Fmoc-protected dipeptides, Fmoc-Gly-Xxx-OY/Fmoc-Xxx-Gly-OY (Xxx = Ala, Val, Leu, Phe) and Fmoc-Ala-Xxx-OY/Fmoc-Xxx-Ala-OY (Xxx = Leu, Phe) (Fmoc = [(9-fluorenylmethyl) oxy]carbonyl) and Y = CH3/H), have been characterized and differentiated by both positive and negative ion electrospray ionization ion-trap tandem mass spectrometry (ESI-IT-MSn). In contrast to the behavior of reported unprotected dipeptide isomers which mainly produce y 1+ and/or a1+ ions, the protonated Fmoc-Xxx-Gly-OY, Fmoc-Ala-Xxx-OY and Fmoc-Xxx-Ala-OY yield significant b 1+ ions. These ions are formed, presumably with stable protonated aziridinone structures. However, the peptides with Gly- at the N-terminus do not form b1+ ions. The [M + H]+ ions of all the peptides undergo a McLafferty-type rearrangement followed by loss of CO2 to form [M + H-Fmoc + H]+. The MS3 collision-induced dissociation (CID) of these ions helps distinguish the pairs of isomeric dipeptides studied in this work. Further, negative ion MS 3 CID has also been found to be useful for differentiating these isomeric peptide acids. The MS3 of [M-H-Fmoc + H]- of isomeric peptide acids produce c1-, z1 - and y1- ions. Thus the present study of Fmoc-protected peptides provides additional information on mass spectral characterization of the dipeptides and distinguishes the positional isomers. Copyright
Synthesis of ureidopeptides using pentafluorophenyl carbamates from N a-Fmoc-peptide acids
Sureshbabu, Vommina V.,Venkataramanarao, Rao
, p. 910 - 919 (2008/12/23)
Highly active and shelf stable pentafluoro phenol derived Fmoc-peptidyl carbamates have been synthesized from corresponding Fmoc-peptidyl isocyanates. The utility of pentafluorophenyl carbamate intermediates has been demonstrated by the synthesis of tri, penta and hexapeptidyl ureas which are obtained in good yields. All the synthesised compounds have been characterized by 1H NMR, 13C NMR and mass spectroscopy. The coupling reaction using pentafluorophenyl carbamates to insert urea bond between α amino acids is fast, clean and high yielding.
Carboxylate protective groups, a process for their preparation, their coupling to a functional group, and their use
-
, (2008/06/13)
Carboxylates of polar, hydrophilic alcohols of the formula STR1 in which R is an unbranched or branched organic radical which contains, as polar members between aliphatic or araliphatic hydrocarbon bridges, ether oxygens, amine nitrogen groups or a mixture of ether and amine groups which can be incorporated into a cyclic structure, where the total length does not exceed 20 members and where, in the case of polyethylene glycol [(CH2 --CH2 --O)n ], n indicates the number of the members and is defined as any integer, and R' is an aliphatic or araliphatic radical which has at least one functional group, are suitable as protective groups since they can be introduced selectively into functional groups of organic compounds and eliminated specifically by lipases.
SYNTHESIS OF HUMAN M BLOOD GROUP ANTIGENIC GLYCOPEPTIDE
Nakahara, Yoshiaki,Iijima, Hiroyuki,Ogawa, Tomoya
, p. 3321 - 3324 (2007/10/02)
A first total synthesis of terminal glycoheptapeptide of human glycophorin AM was accomplished by solution phase peptide condensation utilizing the tetrasaccharide-linked amino acid building blocks designed for Fmoc strategy.
