The majority of protein-based biopharmaceuticals approved or in clinical trials bear some form of post-translational modification (PTM), which can profoundly affect protein properties relevant to their therapeutic application. Whereas glycosylation represents the most common modification, additional PTMs, including carboxylation, hydroxylation, sulfation and amidation, are characteristic of some products. The relationship between structure and function is understood for many PTMs but remains incomplete for others, particularly in the case of complex PTMs, such as glycosylation. A better understanding of such structural-functional relationships will facilitate the development of second-generation products displaying a PTM profile engineered to optimize therapeutic usefulness.

No abstract

No abstract

No abstract

No abstract

No abstract

The rate of biopharmaceutical approvals has leveled off, but some milestones bode well for the future.

1Whey is a highly polluting by-product of cheese and casein powder manufacturing with 2 worldwide production of whey is estimated at around 190×10 6 ton/year and growing. Historically 3 whey was considered a burdensome, environmentally damaging by-product. In the last decades 4 however, much research has gone into finding viable alternatives for whey rather than just 5 disposing of it. Multiple biotechnological avenues have been explored and in some cases 6 exploited to turn this waste product into a valuable commodity. Avenues explored include 7 traditional uses of whey as both an animal and human food to the more advanced uses such as 8 the use of whey protein as health promoters and the potential of whey to be used as a feed stock 9to manufacture a whole range of useful substances e.g. ethanol. 10