Structural and Functional Role of Proline Residues in Fibroblast Growth Factor-1

Additional file 4: Figure S2. Electrolyte leakage of MsK8 cells (A) upon inoculation with Phytophthora zoospores (zsp) or (B) treatment with zoospore exudate (ZE) measured as conductivity at various time points. Colors of the bars represent a specific species and/or strain as indicated and correspond to the colors in Fig. 2. Error bars represent standard deviation (n = 3)

Heparin affinity tag and application thereof

In one aspect, affinity tags for recombinant protein purification are described herein which, in some embodiments, can mitigate or overcome disadvantages of prior affinity tag systems. In some embodiments, for example, affinity tags described herein permit efficient elution of desired recombinant proteins with simplified solution systems, such as alkali metal salt solutions. An affinity tag described herein comprises an amino acid sequence including a repeating amino acid unit of BXXXBXX, wherein B is an amino acid selected from the group consisting of histidine, lysine and arginine and X is an amino acid selected from the group consisting of amino acids other than histidine, lysine and arginine

Heparin affinity tag and applications thereof

In one aspect, affinity tags for recombinant protein purification are described herein which, in some embodiments, can mitigate or overcome disadvantages of prior affinity tag systems. In some embodiments, for example, affinity tags described herein permit efficient elution of desired recombinant proteins with simplified solution systems, such as alkali metal salt solutions. An affinity tag described herein comprises an amino acid sequence including a repeating amino acid unit of BXXXBXX, wherein B is an amino acid selected from the group consisting of histidine, lysine and arginine and X is an amino acid selected from the group consisting of amino acids other than histidine, lysine and arginin

Peptides with antifungal activity and methods of using the peptides

Compositions with antifungal activity and methods of using such compositions are provided herein. In particular the compositions are peptides of SEQ ID NO: 1 and variations thereof. The peptides may contain L or D amino acids and may be circularized, dimerized or otherwise modified to make the compositions resistant to proteolysis. The compositions may be used to inhibit microbial growth and in particular fungal growth

Cleavage resistant photoluminescent proteins and applications thereof

Photoluminescent proteins resistant to protein cleavage reagents are described herein. In being resistant to cleavage reagents, such photoluminesncent proteins can reduce the number of digestion or cleavage products, thereby simplifying quantification and purification of recombinant protein compositions. In some embodiments, a photoluminescent protein described herein comprises an amino acid sequence having an absence of internal methionine residues

Engineered FGF compositions and methods of use thereof

The present invention relates to the development of stable mutants of FGF-1 and FGF-2. In particular, it relates to novel engineered FGF-1 and FGF-2 polypeptides as well as polynucleotides, DNA constructs, and vectors encoding such polypeptides. In another aspect, pharmaceutical compositions and hydrogels including the disclosed polypeptides, polynucleotides, DNA constructs, and vectors are provided. In a still further aspect, methods of treating conditions using the compositions disclosed herein are provided

Modulation of Interleukin-12 activity in the presence of heparin

Glycosaminoglycans (GAGs), especially heparin and heparan sulfate (HS), modulate the functions of numerous cytokines. The aims of this multidisciplinary research were to characterize heparin binding to interleukin-12 (IL-12) and determine the mechanism(s) by which heparin influences IL-12 bioactivity. Heparin and HS were found to bind human IL-12 (hIL-12) with low micromolar affinity and increase hIL-12 bioactivity by more than 6-fold. Conversely, other GAGs did not demonstrate significant binding, nor did their addition affect hIL-12 bioactivity. Biophysical studies demonstrated that heparin induced only minor conformational changes while size-exclusion chromatography and small angle X-ray scattering studies indicated that heparin induced dimerization of hIL-12. Heparin modestly protected hIL-12 from proteolytic degradation, however, this was not a likely mechanism for increased cytokine activity in vitro. Flow cytometry studies revealed that heparin increased the amount of hIL-12 bound to cell surfaces. Heparin also facilitated hIL-12 binding and signaling in cells in which both hIL-12 receptor subunits were functionally deleted. Results of this study demonstrate a new role for heparin in modulating the biological activity of IL-12