rfhSP-D consists of two parts, the anti-inflammatory functional binding domain and the trimerising neck region of the full length molecule. rfhSP-D lacks the majority of the collagen domain. Whilst maintaining many of the functions of the native protein, development of the fragment has many advantages as it is:
- Functional as an anti-inflammatory
- Easier to manufacture in high yields
- Easier to handle as it is extremely soluble, does not aggregate
- It can by lyophilized or frozen/thawed
- Produced as a trimer and does not oligermerzie like the full length molecule
Development of this fragment thus now makes it feasible for developing an SP-D based protien for prevention of lung diseases. This molecule is well characterised both structurally and functionally (in-vitro and in relevant pre-clinical models). We, and others, have clearly demonstrated that rfhSP-D protects the lung against infections and other noxious stimuli, and prevents chronic inflammation and the development of emphysema and fibrosis, which are the key pathological features of nCLD.