Chemical modification of proteins - challenges and trends at the start of the 2020s
Publikation: Bidrag til tidsskrift › Review › Forskning › fagfællebedømt
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Chemical modification of proteins - challenges and trends at the start of the 2020s. / Fischer, Niklas Henrik; Oliveira, Maria Teresa; Diness, Frederik.
I: Biomaterials Science, Bind 11, Nr. 3, 2023, s. 719–748.Publikation: Bidrag til tidsskrift › Review › Forskning › fagfællebedømt
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TY - JOUR
T1 - Chemical modification of proteins - challenges and trends at the start of the 2020s
AU - Fischer, Niklas Henrik
AU - Oliveira, Maria Teresa
AU - Diness, Frederik
PY - 2023
Y1 - 2023
N2 - Ribosomally expressed proteins perform multiple, versatile, and specialized tasks throughout Nature. In modern times, chemically modified proteins, including improved hormones, enzymes, and antibody-drug-conjugates have become available and have found advanced industrial and pharmaceutical applications. Chemical modification of proteins is used to introduce new functionalities, improve stability or drugability. Undertaking chemical reactions with proteins without compromising their native function is still a core challenge as proteins are large conformation dependent multifunctional molecules. Methods for functionalization ideally should be chemo-selective, site-selective, and undertaken under biocompatible conditions in aqueous buffer to prevent denaturation of the protein. Here the present challenges in the field are discussed and methods for modification of the 20 encoded amino acids as well as the N-/C-termini and protein backbone are presented. For each amino acid, common and traditional modification methods are presented first, followed by more recent ones.
AB - Ribosomally expressed proteins perform multiple, versatile, and specialized tasks throughout Nature. In modern times, chemically modified proteins, including improved hormones, enzymes, and antibody-drug-conjugates have become available and have found advanced industrial and pharmaceutical applications. Chemical modification of proteins is used to introduce new functionalities, improve stability or drugability. Undertaking chemical reactions with proteins without compromising their native function is still a core challenge as proteins are large conformation dependent multifunctional molecules. Methods for functionalization ideally should be chemo-selective, site-selective, and undertaken under biocompatible conditions in aqueous buffer to prevent denaturation of the protein. Here the present challenges in the field are discussed and methods for modification of the 20 encoded amino acids as well as the N-/C-termini and protein backbone are presented. For each amino acid, common and traditional modification methods are presented first, followed by more recent ones.
KW - EXTRINSIC CROSS-LINK
KW - SELECTIVE BIOCONJUGATION
KW - RIBONUCLEASE-A
KW - DUAL FUNCTIONALIZATION
KW - REDUCTIVE ALKYLATION
KW - HISTIDINE-RESIDUES
KW - N-ETHYLMALEIMIDE
KW - FOLDING PATHWAY
KW - CLICK LIGATION
KW - AMINO-GROUPS
U2 - 10.1039/d2bm01237e
DO - 10.1039/d2bm01237e
M3 - Review
C2 - 36519403
VL - 11
SP - 719
EP - 748
JO - Biomaterials Science
JF - Biomaterials Science
SN - 2047-4830
IS - 3
ER -
ID: 330840882