PMC:7795856 / 14285-14970 JSONTXT

{"project":"LitCovid-PubTator","denotations":[{"id":"262","span":{"begin":263,"end":270},"obj":"Species"},{"id":"263","span":{"begin":629,"end":636},"obj":"Species"}],"attributes":[{"id":"A262","pred":"tao:has_database_id","subj":"262","obj":"Tax:562"},{"id":"A263","pred":"tao:has_database_id","subj":"263","obj":"Tax:562"}],"namespaces":[{"prefix":"Tax","uri":"https://www.ncbi.nlm.nih.gov/taxonomy/"},{"prefix":"MESH","uri":"https://id.nlm.nih.gov/mesh/"},{"prefix":"Gene","uri":"https://www.ncbi.nlm.nih.gov/gene/"},{"prefix":"CVCL","uri":"https://web.expasy.org/cellosaurus/CVCL_"}],"text":"The present data demonstrate that the PASylation technology can solve two major problems of a peptide drug: (i) instability in the expression host and (ii) low bioactivity due to fast renal clearance. Typically, small peptides, if expressed in a soluble state in E. coli, are quickly degraded by host cell proteases [42] and, thus, require production as larger fusion proteins as well as subsequent release by site-specific cleavage in vitro. Here, fusion with a random-coil forming PAS sequence of ~600 amino acids prevented proteolytic degradation and allowed cost-efficient one-step production of the intact fusion protein in E. coli without the need of additional processing steps."}

{"project":"LitCovid-sentences","denotations":[{"id":"T89","span":{"begin":0,"end":200},"obj":"Sentence"},{"id":"T90","span":{"begin":201,"end":442},"obj":"Sentence"},{"id":"T91","span":{"begin":443,"end":685},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"The present data demonstrate that the PASylation technology can solve two major problems of a peptide drug: (i) instability in the expression host and (ii) low bioactivity due to fast renal clearance. Typically, small peptides, if expressed in a soluble state in E. coli, are quickly degraded by host cell proteases [42] and, thus, require production as larger fusion proteins as well as subsequent release by site-specific cleavage in vitro. Here, fusion with a random-coil forming PAS sequence of ~600 amino acids prevented proteolytic degradation and allowed cost-efficient one-step production of the intact fusion protein in E. coli without the need of additional processing steps."}