48065-82-3Relevant academic research and scientific papers
A genetically encoded aza-michael acceptor for covalent cross-linking of protein-receptor complexes
Furman, Jennifer L.,Kang, Mingchao,Choi, Seihyun,Cao, Yu,Wold, Erik D.,Sun, Sophie B.,Smider, Vaughn V.,Schultz, Peter G.,Kim, Chan Hyuk
, p. 8411 - 8417 (2014)
Selective covalent bond formation at a protein-protein interface potentially can be achieved by genetically introducing into a protein an appropriately tuned electrophilic unnatural amino acid that reacts with a native nucleophilic residue in its cognate receptor upon complex formation. We have evolved orthogonal aminoacyl-tRNA synthetase/tRNACUA pairs that genetically encode three aza-Michael acceptor amino acids, Nε- acryloyl-(S)-lysine (AcrK, 1), p-acrylamido-(S)-phenylalanine (AcrF, 2), and p-vinylsulfonamido-(S)-phenylalanine (VSF, 3), in response to the amber stop codon in Escherichia coli. Using an αErbB2 Fab-ErbB2 antibody-receptor pair as an example, we demonstrate covalent bond formation between an αErbB2-VSF mutant and a specific surface lysine ε-amino group of ErbB2, leading to near quantitative cross-linking to either purified ErbB2 in vitro or to native cellular ErbB2 at physiological pH. This efficient biocompatible reaction may be useful for creating novel cell biological probes, diagnostics, or therapeutics that selectively and irreversibly bind a target protein in vitro or in living cells.
Method for a convenient and efficient synthesis of amino acid acrylic monomers with zwitterionic structure
Nagaoka, Shoji,Shundo, Atsuomi,Satoh, Takao,Nagira, Kazuhiko,Kishi, Ryoich,Ueno, Katsuhiko,Iio, Kokoro,Ihara, Hirotaka
, p. 2529 - 2534 (2005)
Ampholyte monomers with zwitterionic moiety derived from α-amino acid, that is, L-lysine and L-serine, were obtained using a method in which their copper complexes could be produced in simple steps. The N-acryloylation of L-lysine and L-serine was carried out by reaction between their copper complexes and acryloyl chloride. Specifically, the removal of copper from the copper complex of acryloyl amino acid through the use of 8-hydroxyquinoline as an organic chelate precipitant increased the yield of the ampholyte monomers with zwitterionic moiety. These syntheses were easily carried out in a three-step procedure. Copyright Taylor & Francis, Inc.
Strength-tunable printing of xanthan gum hydrogel: Via enzymatic polymerization and amide bioconjugation
Pan, Hui,Zheng, Bolin,Shen, Hongdou,Qi, Meiyuan,Shang, Yinghui,Wu, Chu,Zhu, Rongrong,Cheng, Liming,Wang, Qigang
, p. 3457 - 3460 (2020)
Amide bioconjugation and interfacial enzyme polymerization are designed to provide a general strategy for regulating the mechanical strength (storage modulus from 3 kPa to 100 kPa) of printable hydrogel inks.
BIOCOMPATIBLE POLYMERIC DRUG CARRIERS FOR DELIVERING ACTIVE AGENTS
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Page/Page column 43, (2021/05/07)
The present disclosure relates to the delivery of multiple copies of a payload molecule such as an active agent or a chelating agent capable of capturing an active agent, using as a carrier for their delivery a biocompatible copolymer comprising side chain-linked amino acids functionalized at their alpha-amino group by a reactive azide moiety by means of which the payload molecules are coupled to the copolymer. The copolymer is typically further functionalized to contain a single copy of a cell type- or tissue type-specific targeting moiety.
A GENETICALLY ENCODED, PHAGE-DISPLAYED CYCLIC PEPTIDE LIBRARY AND METHODS OF MAKING THE SAME
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Paragraph 0094; 00117-00118; 00120-00122, (2020/12/07)
Embodiments of the present disclosure pertain to methods of selecting cyclic peptides that bind to a target by transforming a phage display library with a plurality of nucleic acids into bacterial host cells, where the nucleic acids include phage coat protein genes with a combinatorial region that encodes at least one cysteine and at least one non-canonical amino acid. The transformation results in the production of phage particles with phage coat proteins where the cysteine and the non-canonical amino acid couple to one another to form a cyclic peptide library. Phage particles are then screened against the desired target to select bound cyclic peptides. Amino acid sequences of the selected cyclic peptides are then identified. Additional embodiments pertain to methods of constructing a phage display library that encodes the cyclic peptides. Further embodiments of the present disclosure pertain to the produced cyclic peptides, phage display libraries and phage particles.
New polymer materials for contact lens applications
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Paragraph 0077-0078, (2020/09/22)
The present invention relates to copolymers made from a polymerization mixture comprising (a) one or more polymerizable monomers, which monomers are characterized as having at least one vinylic group and not containing an amino acid residue, (b) one or mo
PROXIMITY INDUCED SITE-SPECIFIC ANTIBODY CONJUGATION
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Page/Page column 24, (2019/11/28)
The present disclosure provides methods for proximity-induced antibody conjugation of target agents).
A Genetically Encoded, Phage-Displayed Cyclic-Peptide Library
Wang, Xiaoshan Shayna,Chen, Peng-Hsun Chase,Hampton, J. Trae,Tharp, Jeffery M.,Reed, Catrina A.,Das, Sukant K.,Wang, Duen-Shian,Hayatshahi, Hamed S.,Shen, Yang,Liu, Jin,Liu, Wenshe Ray
supporting information, p. 15904 - 15909 (2019/10/28)
Superior to linear peptides in biological activities, cyclic peptides are considered to have great potential as therapeutic agents. To identify cyclic-peptide ligands for therapeutic targets, phage-displayed peptide libraries in which cyclization is achieved by the covalent conjugation of cysteines have been widely used. To resolve drawbacks related to cysteine conjugation, we have invented a phage-display technique in which its displayed peptides are cyclized through a proximity-driven Michael addition reaction between a cysteine and an amber-codon-encoded N?-acryloyl-lysine (AcrK). Using a randomized 6-mer library in which peptides were cyclized at two ends through a cysteine–AcrK linker, we demonstrated the successful selection of potent ligands for TEV protease and HDAC8. All selected cyclic peptide ligands showed 4- to 6-fold stronger affinity to their protein targets than their linear counterparts. We believe this approach will find broad applications in drug discovery.
Aldehyde-mediated bioconjugation: Via in situ generated ylides
Parmar, Sangeeta,Pawar, Sharad P.,Iyer, Ramkumar,Kalia, Dimpy
supporting information, p. 14926 - 14929 (2019/12/24)
A technically simple approach for rapid, high-yielding and site-selective bioconjugation has been developed for both in vitro and cellular applications. This method involves the generation of maleimido-phosphonium ylides via 4-nitrophenol catalysis under physiological conditions followed by their Wittig reactions with aldehyde-appended biomolecules.
Preparation, characterization, and biocompatibility evaluation of poly(Nε-acryloyl-l-lysine)/hyaluronic acid interpenetrating network hydrogels
Cui, Ning,Qian, Junmin,Xu, Weijun,Xu, Minghui,Zhao, Na,Liu, Ting,Wang, Hongjie
, p. 1017 - 1026 (2015/10/29)
In the present study, poly(Nε-acryloyl-l-lysine)/hyaluronic acid (pLysAAm/HA) interpenetrating network (IPN) hydrogels were successfully fabricated through the combination of hydrazone bond crosslinking and photo-crosslinking reactions. The HA hydrogel network was first synthesized from 3,3′-dithiodipropionate hydrazide-modified HA and polyethylene glycol dilevulinate by hydrazone bond crosslinking. The pLysAAm hydrogel network was prepared from Nε-acryloyl-l-lysine and N,N′-bis(acryloyl)-(l)-cystine by photo-crosslinking. The resultant pLysAAm/HA hydrogels had a good shape recovery property after loading and unloading for 1.5 cycles (up to 90%) and displayed a highly porous microstructure. Their compressive moduli were at least 5 times higher than that of HA hydrogels. The pLysAAm/HA hydrogels had an equilibrium swelling ratio of up to 37.9 and displayed a glutathione-responsive degradation behavior. The results from in vitro biocompatibility evaluation with pre-osteoblasts MC3T3-E1 cells revealed that the pLysAAm/HA hydrogels could support cell viability and proliferation. Hematoxylin and eosin staining indicated that the pLysAAm/HA hydrogels allowed cell and tissue infiltration, confirming their good in vivo biocompatibility. Therefore, the novel pLysAAm/HA IPN hydrogels have great potential for bone tissue engineering applications.
