169624-67-3Relevant articles and documents
Searching for improved mimetic peptides inhibitors preventing conformational transition of amyloid-β42 monomer
Gera, János,Sz?gi, Titanilla,Bozsó, Zsolt,Fül?p, Livia,Barrera, Exequiel E.,Rodriguez, Ana M.,Méndez, Luciana,Delpiccolo, Carina M.L.,Mata, Ernesto G.,Cioffi, Federica,Broersen, Kerensa,Paragi, Gabor,Enriz, Ricardo D.
, p. 211 - 221 (2018/08/24)
A series of novel mimetic peptides were designed, synthesised and biologically evaluated as inhibitors of Aβ42 aggregation. One of the synthesised peptidic compounds, termed compound 7 modulated Aβ42 aggregation as demonstrated by thioflavin T fluorescence, acting also as an inhibitor of the cytotoxicity exerted by Aβ42 aggregates. The early stage interaction between compound 7 and the Aβ42 monomer was investigated by replica exchange molecular dynamics (REMD) simulations and docking studies. Our theoretical results revealed that compound 7 can elongate the helical conformation state of an early stage Aβ42 monomer and it helps preventing the formation of β-sheet structures by interacting with key residues in the central hydrophobic cluster (CHC). This strategy where early “on-pathway” events are monitored by small molecules will help the development of new therapeutic strategies for Alzheimer's disease.
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
, 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
Potential formation of intramolecular inclusion complexes in peptidocyclodextrins as evidenced by NMR spectroscopy
Djedaini-Pilard, Florence,Azaroual-Bellanger, Nathalie,Gosnat, Muriel,Vernet, Delphine,Perly, Bruno
, p. 723 - 730 (2007/10/02)
Investigations of the structure of β- and γ-cyclodextrin derivatives in solution obtained by grafting amino acids or peptides are presented.These compounds are models for vectorization-dedicated molecular carriers.It is shown that for some amino acids, strong intramolecular self-inclusion complexes are formed in aqueous solution.This process strongly depends upon the nature and position of the pertinent amino acid in the peptide sequence.Two dimensional NMR experiments are used in conjunction with competition with external guests to evidence and estimate the strength of these auto-inclusion complexes.
