Total synthesis of the α-subunit of human glycoprotein hormones: Toward fully synthetic homogeneous human follicle-stimulating hormone Journal Article
| Authors: | Aussedat, B.; Fasching, B.; Johnston, E.; Sane, N.; Nagorny, P.; Danishefsky, S. J. |
| Article Title: | Total synthesis of the α-subunit of human glycoprotein hormones: Toward fully synthetic homogeneous human follicle-stimulating hormone |
| Abstract: | Described herein is the first total chemical synthesis of the unique α-subunit of the human glycoprotein hormone (α-hGPH). Unlike the biologically derived glycoprotein hormones, which are isolated as highly complex mixtures of glycoforms, α-hGPH obtained by chemical synthesis contains discrete homogeneous glycoforms. Two such systems have been prepared. One contains the disaccharide chitobiose at the natural N-glycosylation sites. The other contains dodecamer oligosaccharides at these same sites. The dodecamer sugar is a consensus sequence incorporating the key features associated with human glycoproteins. © 2012 American Chemical Society. |
| Keywords: | unclassified drug; carboxy terminal sequence; glycosylation; sugars; chemical structure; alpha chain; glycoproteins; glycoprotein; synthesis; key feature; total synthesis; chemical synthesis; asparagine; chitobiose; follicle stimulating hormone; glycoprotein hormones; hormones; follitropin; glycoforms; reaction time; oligosaccharide; consensus sequence; complex mixture; dodecamer; n-glycosylation sites; alpha human glycoprotein hormone |
| Journal Title: | Journal of the American Chemical Society |
| Volume: | 134 |
| Issue: | 7 |
| ISSN: | 0002-7863 |
| Publisher: | American Chemical Society |
| Date Published: | 2012-02-22 |
| Start Page: | 3532 |
| End Page: | 3541 |
| Language: | English |
| DOI: | 10.1021/ja2111459 |
| PROVIDER: | scopus |
| PMCID: | PMC3288947 |
| PUBMED: | 22280541 |
| DOI/URL: | |
| Notes: | --- - "Export Date: 2 April 2012" - "CODEN: JACSA" - "Source: Scopus" |
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