TY - JOUR
T1 - Sortase a mediated protein modifications and peptide conjugations
AU - Voloshchuk, Natalya
AU - Liang, Danni
AU - Liang, Jun F.
N1 - Publisher Copyright:
© 2015 Bentham Science Publishers.
PY - 2015/12/1
Y1 - 2015/12/1
N2 - Bioactive peptides regulate many physiological processes, acting at some sites as endocrine or paracrine signals and at others as neurotransmitters or growth factors, and show useful properties for human health, including antimicrobial, antifungal, antiviral, and antitumor activities. Although most peptides can be produced using the molecular biology approach, they are produced in limited quantities at high costs and associated with some difficulties in purification and isolation. In addition, some peptides with special structures, such as cyclic peptides, can hardly be produced by the biological method. This is especially true for the biomedical applications in which long peptides with many repeated functional sequences are usually needed. Prokaryotic transpeptidase Sortase A mediates sequence specific peptide ligation and represents a new method for peptide modifications. Besides peptide and protein modifications to improve stability and specificity of therapeutic peptides, Sortase A mediated peptide ligation has been extended to wider applications such as molecular sensing, surface modification, and biomaterials. In this review, we will focus the pharmacological applications of Sortase A for the production of nucleic acid-peptide conjugates, glycosylated peptides, modified proteins/antibodies, and cyclic peptides.
AB - Bioactive peptides regulate many physiological processes, acting at some sites as endocrine or paracrine signals and at others as neurotransmitters or growth factors, and show useful properties for human health, including antimicrobial, antifungal, antiviral, and antitumor activities. Although most peptides can be produced using the molecular biology approach, they are produced in limited quantities at high costs and associated with some difficulties in purification and isolation. In addition, some peptides with special structures, such as cyclic peptides, can hardly be produced by the biological method. This is especially true for the biomedical applications in which long peptides with many repeated functional sequences are usually needed. Prokaryotic transpeptidase Sortase A mediates sequence specific peptide ligation and represents a new method for peptide modifications. Besides peptide and protein modifications to improve stability and specificity of therapeutic peptides, Sortase A mediated peptide ligation has been extended to wider applications such as molecular sensing, surface modification, and biomaterials. In this review, we will focus the pharmacological applications of Sortase A for the production of nucleic acid-peptide conjugates, glycosylated peptides, modified proteins/antibodies, and cyclic peptides.
KW - Antibody
KW - Conjugation
KW - Cyclic peptide
KW - Lipid
KW - Peptide nucleic acid
KW - Peptides
KW - Sortase A
KW - Surface modification
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U2 - 10.2174/1570163812666150903115601
DO - 10.2174/1570163812666150903115601
M3 - Article
C2 - 26333952
AN - SCOPUS:84958671538
SN - 1570-1638
VL - 12
SP - 205
EP - 213
JO - Current Drug Discovery Technologies
JF - Current Drug Discovery Technologies
IS - 4
ER -