228245-16-7Relevant academic research and scientific papers
Peptide microarrays for the determination of protease substrate specificity
Salisbury, Cleo M.,Maly, Dustin J.,Ellman, Jonathan A.
, p. 14868 - 14870 (2002)
A method is described for the preparation of substrate microarrays that allow for the rapid determination of protease substrate specificity. Peptidyl coumarin substrates, synthesized on solid support using standard techniques, are printed onto glass slide
A hydroxylamine probe for profiling: S-acylated fatty acids on proteins
Schulte-Zweckel, Janine,Dwivedi, Mridula,Brockmeyer, Andreas,Janning, Petra,Winter, Roland,Triola, Gemma
, p. 11183 - 11186 (2019/09/30)
Reversible S-palmitoylation is a key regulatory mechanism of protein function and localization. There is increasing evidence that S-acylation is not restricted to palmitate but it includes shorter, longer, and unsaturated fatty acids. However, the diversity of this protein modification has not been fully explored. Herein, we report a chemical probe that combined with MS-based analysis allows the rapid detection and quantification of fatty acids linked to proteins. We have used this approach to profile the S-acylome and to show that the oncogene N-Ras is heterogeneously acylated with palmitate and palmitoleate. Studies on protein distribution in membrane subdomains with semisynthetic proteins revealed that unsaturated N-Ras presents an increased tendency toward clustering and higher insertion kinetic rate constants.
FLUORESCENT PROBES FOR ABASIC SITE DETECTION
-
, (2016/11/02)
A fluorescent probe for binding to and detection of AP sites of DNA includes the following formula: F-L-X where F is a fluorescent moiety, X is an aminooxy group (-ONH2), and L is a linker that links or couples the fluorescent moiety to the oxy
COMPOSITIONS CONTAINING, METHODS INVOLVING, AND USES OF NON-NATURAL AMINO ACIDS AND POLYPEPTIDES
-
Paragraph 0638, (2016/07/27)
Disclosed herein are non-natural amino acids and polypeptides that include at least one non-natural amino acid, and methods for making such non-natural amino acids and polypeptides. The non-natural amino acids, by themselves or as a part of a polypeptide, can include a wide range of possible functionalities, but typical have at least one oxime, carbonyl, dicarbonyl, and/or hydroxylamine group. Also disclosed herein are non-natural amino acid polypeptides that are further modified post-translationally, methods for effecting such modifications, and methods for purifying such polypeptides. Typically, the modified non-natural amino acid polypeptides include at least one oximine, carbonyl, dicarbonyl, and/or hydroxylamine group. Further disclosed are methods for using such non-natural amino acid polypeptides and modified non-natural amino acid polypeptides, including therapeutic, diagnostic, and other biotechnology uses.
Designer macrocyclic organo-peptide hybrids inhibit the interaction between p53 and HDM2/X by accommodating a functional α-helix
Smith, Jessica M.,Frost, John R.,Fasan, Rudi
supporting information, p. 5027 - 5030 (2014/05/06)
We report the design of side-chain-to-tail linked organo-peptide hybrids incorporating an α-helical protein-binding motif. Using this strategy, macrocyclic inhibitors of the p53:HDM2 interaction displaying dual specificity against the HDMX homolog as well
Thermosensitive peptide-hybrid ABC block copolymers obtained by ATRP: Synthesis, self-assembly, and enzymatic degradation
De Graaf, Albert J.,Mastrobattista, Enrico,Vermonden, Tina,Van Nostrum, Cornelus F.,Rijkers, Dirk T.S.,Liskamp, Rob M.J.,Hennink, Wim E.
, p. 842 - 851 (2012/05/31)
Peptide-hybrid ABC block copolymers were synthesized by growing two different polymer chains from a native peptide using atom transfer radical polymerization (ATRP). To this end, two different ATRP initiators were coupled via orthogonal methods to the N- and C-terminus of the peptide Ser-Gly-Pro-Gln-Gly-Ile-Phe-Gly-Gln-Met-Gly, a substrate for matrix metalloproteases 2 and 9. First, a hydrophilic block of poly(oligo(ethylene glycol) methyl ether methacrylate) (pOEGMA) was polymerized from the peptide's C-terminus. Before polymerization of the second block, the first living chain end was inactivated by substitution of its Cl-terminus with azide under mild conditions. Then, a thermosensitive block of poly(N-isopropylacrylamide) (pNIPAm) was polymerized from the peptide's N-terminus. Well-defined polymers were obtained with good control over both block sizes. The resulting polymers self-assembled into micelles above the cloud point of the pNIPAm block. As anticipated, it was shown that the peptide linkage between the polymer blocks can be cut by a metalloprotease, leading to "shedding" of the corona of the micelles which makes these systems potentially suitable for enzyme-triggered drug delivery.
