Pregnancy and Neonatal Outcomes in Gestational Diabetes Treated with Regular Insulin or Fast-Acting Insulin Analogues

2015 ◽  
Vol 81 (3) ◽  
pp. 232-237 ◽  
Author(s):  
Ji Yeon You ◽  
Suk-Joo Choi ◽  
Cheong-Rae Roh ◽  
Jong-Hwa Kim ◽  
Soo-young Oh
2017 ◽  
Author(s):  
Dayana Cabral da Silva ◽  
Luís Maurício T. R. Lima

ABSTRACTSince the discovery of amylin its use has been discouraged by the inadequacy of the protocol involving multiple injections in addition to insulin. While a combined fixed-dose formulation is thus highly desirable, it has long been limited due to incompatibility as historically documented. We have investigated the compatibility of regular and fast-acting insulin analogues (Aspart, AspB28, and LisPro, LysB28ProB29) with the amylin analogue pramlintide. Insulin interacts with pramlintide, forming heterodimers as probed by electrospray ionization - ion mobility spectrometry-mass spectrometry. While their interaction is likely to delay the amyloid aggregation of pramlintide in phosphate-buffered solution pH 7.0, they do not prevent aggregation at this condition. At acidic sodium acetate solution pH 5.0, combination of pramlintide and the fast-acting insulin analogues become stable against amyloid aggregation. The co-formulated product at high concentration of both pramlintide (600 μg/mL,150 μM) and LisPro insulin (50 IU/mL, 300 μM) showed also stability against amyloid aggregation. These data indicate a potential for the development of a co-formulation of fast-acting LisPro insulin with pramlintide, which could bring benefits for the combined therapy.AbbreviationsIAPP,islet amyloid polypeptide;ESI-IMS-MS,Electrospray Ionization–Ion Mobility Spectrometry–Mass Spectrometry.


2013 ◽  
Vol 16 (7) ◽  
pp. A451
Author(s):  
S. Cammarota ◽  
D. Bruzzese ◽  
A.L. Catapano ◽  
A. Citarella ◽  
L. De Luca ◽  
...  

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