484-42-4Relevant articles and documents
HPLC FREE PURIFICATION OF PEPTIDES BY THE USE OF NEW CAPPING AND CAPTURE REAGENTS
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Page/Page column 17; 21, (2020/07/25)
The present disclosure relates to the use of a capping and capture reagent in solid phase peptide synthesis. The present disclosure further relates to a method of solid phase peptide synthesis, wherein a capping and capture reagent according to the present disclosure is used. The present disclosure further relates to a method for purification of a (full-length) synthetic peptide via use of a capping and capture reagent according to the present disclosure. The present disclosure also relates to a kit comprising a capping and capture reagent according to the present disclosure and an amino oxy resin or a hydrazine resin and the use of the kit.
A Vinylogous Photocleavage Strategy Allows Direct Photocaging of Backbone Amide Structure
Mangubat-Medina, Alicia E.,Martin, Samuel C.,Hanaya, Kengo,Ball, Zachary T.
supporting information, p. 8401 - 8404 (2018/06/29)
Side-chain modifications that respond to external stimuli provide a convenient approach to control macromolecular structure and function. Responsive modification of backbone amide structure represents a direct and powerful alternative to impact folding and function. Here, we describe a new photocaging method using histidine-directed backbone modification to selectively modify peptides and proteins at the amide N-H bond. A new vinylogous photocleavage method allows photorelease of the backbone modification and, with it, restoration of function.
Controlled formation of peptide bonds in the gas phase
Lee, Sunyoung,Valentine, Stephen J.,Reilly, James P.,Clemmer, David E.
scheme or table, p. 15834 - 15837 (2011/11/13)
Photoexcitation (using 157 nm vacuum ultraviolet radiation) of proton-bound peptide complexes leads to water elimination and the formation of longer amino acid chains. Thus, it appears that proton-bound dimers are long-lived intermediates along the pathway to peptide formation. Product specificity can be controlled by selection of specific complexes and the incorporation of blocking groups at the N- or C-termini. The product peptide sequences are confirmed using collision-induced dissociation.
