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Folding of bovine growth hormone is consistent with the molten globule hypothesis (1989)

Brems, David N. ; Havel, Henry A.

New York, NY : Wiley-Blackwell

Proteins: Structure, Function, and Genetics 5 (1989), S. 93-95

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ISSN: 0887-3585

Keywords: folding intermediate ; molten globule state ; protein folding ; Chemistry ; Biochemistry and Biotechnology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Medicine

Notes: Previous results from equilibrium and kinetic studies of the folding of bovine growth hormone (bGH) have demonstrated that bGH does not follow a simple two-step folding mechanism. These results are summarized and interpreted according to the “molten globule” model. The molten globule state of bGH is characterized as a folding intermediate which largely a-helical, retains a compact hydrodynamic radius, has packing of the aromatic side chains that is similar to the unfolded state, and possesses a solvent-exposed hydrophobic surface along helix 106127 that readily leads association.

Additional Material: 1 Ill.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1002/prot.340050110

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PEGylation Prevents the N-Terminal Degradation of Megakaryocyte Growth and Development Factor (1998)

Guerra, Patricia I. ; Acklin, Christine ; Kosky, Andrew A. ; [et al.]

Springer

Pharmaceutical research 15 (1998), S. 1822-1827

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ISSN: 1573-904X

Keywords: cytokine ; rHuMGDF ; PEGylation ; diketopiperazine ; stability

Source: Springer Online Journal Archives 1860-2000

Topics: Chemistry and Pharmacology

Notes: Abstract Purpose. Determine the effect of PEGylation on in-vitro degradation for recombinant human Megakaryocyte Growth and Development Factor (rHuMGDF) in the neutral pH range. Methods. Degradation products were characterized by cation-exchange HPLC, N-terminal sequencing and mass spectrometry. Results. The main route of degradation was through non-enzymatic cyclization of the first two amino acids and subsequent cleavage to form a diketopiperazine and des(Ser, Pro)rHuMGDF. This reaction was prevented by alkylation of the N-terminus by polyethylene glycol (PEG). Conclusions. PEGylation of proteins is commonly performed to achieve increased in-vivo circulation half-lives. For rHuMGDF, an additional advantage of PEGylation was enhancedin-vitro shelf-life stability.