BEGIN:VCALENDAR VERSION:2.0 PRODID:-//jEvents 2.0 for Joomla//EN CALSCALE:GREGORIAN METHOD:PUBLISH BEGIN:VEVENT UID:2691fb41b3b0db5d3cba55fee4e819bd CATEGORIES:Colloquium CREATED:20190905T170150 SUMMARY:Professor Inchan Kwon LOCATION:CCB Auditorium (1303) DESCRIPTION:
“Site-spec ific Albumination for the Prolonged Serum Half-life of Therapeutic Pr oteins”
Therapeutic proteins ha ve been widely used to treat various human diseases. However, short half-li ves of proteins in vivo have often limited developing new proteins and expe nding applications of existing therapeutic proteins. Conjugation of poly et hyleneglycol (PEG) was a conventional strategy to prolong half-life of ther apeutic proteins in vivo. However, PEG conjugation raised several concerns, such as accumulation in vivo and immunogenicity. As an emerging half-life extender alternative to PEG, human serum albumin (HSA) received a great att ention thanks to its exceptionally long half-life (over three weeks). We ac hieved the site-specific conjugation of HSA to therapeutic protein using st rain-promoted azide alkyne cycloaddition (SPAAC) and site-specific incorpor ation of p-azidophenylalanine, resulting in the substantially prolonged ser um half-life in vivo. Fatty acids are natural albumin ligands. Albumin bind ing domains are short peptides with a high affinity to albumin. We also dem onstrated the site-specific conjugation of fatty acid/albumin binding domai n to proteins via click chemistries effectively prolonged serum half-life i n vivo.
~ Coffee/tea will be served prior to lecture ~
X-ALT-DESC;FMTTYPE=text/html:“Site-specific Albumination for the Prolonged Serum Half-lif e of Therapeutic Proteins”
Therapeutic proteins have been widely used to treat various human disease s. However, short half-lives of proteins in vivo have often limited develop ing new proteins and expending applications of existing therapeutic protein s. Conjugation of poly ethyleneglycol (PEG) was a conventional strategy to prolong half-life of therapeutic proteins in vivo. However, PEG conjugation raised several concerns, such as accumulation in vivo and immunogenicity. As an emerging half-life extender alternative to PEG, human serum albumin ( HSA) received a great attention thanks to its exceptionally long half-life (over three weeks). We achieved the site-specific conjugation of HSA to the rapeutic protein using strain-promoted azide alkyne cycloaddition (SPAAC) a nd site-specific incorporation of p-azidophenylalanine, resulting in the su bstantially prolonged serum half-life in vivo. Fatty acids are natural albu min ligands. Albumin binding domains are short peptides with a high affinit y to albumin. We also demonstrated the site-specific conjugation of fatty a cid/albumin binding domain to proteins via click chemistries effectively pr olonged serum half-life in vivo.
~ Coffee/tea will b e served prior to lecture~
X-EXTRAINFO:Hosted by Professor KiBum Lee DTSTAMP:20240328T123202 DTSTART:20190924T150000 DTEND:20190924T160000 SEQUENCE:0 TRANSP:OPAQUE END:VEVENT END:VCALENDAR