Abstract：
:Somatostatin, a natural inhibitor of growth hormone (GH), and its analogs have been used in clinical settings for the treatment of acromegaly, gigantism, thyrotropinoma, and other carcinoid syndromes. However, natural somatostatin is limited for clinical usage because of its short half-life in vivo. Albumin fusion technology was used to construct long-acting fusion proteins and Pichia pastoris was used as an expression system. Three fusion proteins (SS28)(2)-HSA, (SS28)(3)-HSA, and HSA-(SS28)(2), were constructed with different fusion copies of somatostatin-28 and fusion orientations. The expression level of (SS28)(3)-HSA was much lower than (SS28)(2)-HSA and HSA-(SS28)(2) due to the additional fusion of the somatostatin-28 molecule. MALDI-TOF mass spectrometry revealed that severe degradation occurred in the fermentation process. Similar to the standard, somatostatin-14, all three fusion proteins were able to inhibit GH secretion in blood, with (SS28)(2)-HSA being the most effective one. A pharmacokinetics study showed that (SS28)(2)-HSA had a prolonged half-life of 2 h. These results showed that increasing the number of small protein copies fused to HSA may not be a suitable method for improving protein bioactivity.
journal_name
J Ind Microbiol Biotechnoljournal_title
Journal of industrial microbiology & biotechnologyauthors
Ding Y,Fan J,Li W,Peng Y,Yang R,Deng L,Fu Qdoi
10.1007/s10295-014-1440-5subject
Has Abstractpub_date
2014-06-01 00:00:00pages
997-1006issue
6eissn
1367-5435issn
1476-5535journal_volume
41pub_type
杂志文章abstract：:The ability of bacteria to attach to surfaces and develop into a biofilm has been of considerable interest to many groups in numerous industries, including the medical and food industry. However, little is understood in the critical initial step seen in all biofilm development, the initial bacterial cell attachment to...
journal_title：Journal of industrial microbiology & biotechnology
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