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. 2019 Feb 27;9:2978. doi: 10.1038/s41598-019-39776-0

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© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Thermo-analysis and protein aggregation assessment under different thermal and freeze-thaw conditions: (a) DSC thermograms; (b) TG curves of two-state unfolding PASylated Adnectin C and native protein. Samples were prepared in phosphate buffer at pH 6.8 and analyzed in inert atmosphere at a heating rate of 2 °C/min. A negligible shift in both thermograms was observed for PASylated Adnectin C relative to the native protein; (c) aggregation of PASylated Adnectin C and native protein after incubation at the defined temperatures and incubations times. A large increase in A_340nm after heating indicates lower thermal stability. Data are represented as mean ± SD (three replicates). Asterisks denote the significance levels (*p < 0.05, **p < 0.01, and ***p < 0.001); (d,e) DLS of freeze-thaw effect on protein aggregation of the recombinant proteins. Peak shifts were observed for: (d) the native (96.35 nm to 733.7 nm) and (e) PASylated protein (192.3 to 266.6 nm). Lower aggregated forms for PASylated were observed.