Table 1.

Characterization of peptide monomers and their corresponding polymerized ELPs

Pep. No.	Sequencea	Pep. MW (D)	ELPs no.	ELPs MWb (D)	PDIc (Mw/Mn)	DPd	CE%e	Thermal behavior	Topological structure
C	AVHPGVGP	732.8	–	–	–	–	–	–	–
1	QHHPGVGK	858.5	P1	15,400	1.21	17–18	–	UCST	N/Af
2	QHDPGVGK	836.9	P2	17,900	1.28	21–22	–	UCST	N/A
3	QHPGVGHK	858.5	P3	15,500	1.21	18–19	–	UCST	N/A
4	QRLGVGFPK	1000.6	P4	28,000	1.25	27–28	–	UCST	Nanoparticle
5	QRLGVGLPK	966.6	P5	25,200	1.13	26–27	–	UCST	Nanoparticle
6	QRLGVGDPK	968.5	P6	25,500	1.17	26–27	–	UCST	Nanoparticle
7	QVHPGVGK	821.0	P7	29,700	1.29	35–36	–	LCST	Nanoparticle
8	QAPGVGK	754.9	P8	26,400	1.27	34–35	–	–	Random coil
9	QKVPHVGQK	1020.2	P9	–	–	–	90.6%	LCST	Gelg
10	QKAPGVGQK	912.2	P10	–	–	–	89.3%	–	Gel

^aThe conservative sequences in these elastin-repeated units included PGVG, GVGXP, and PHVG. The red colored amino acids inserted are significant in regulating the physicochemical properties of the synthesized ELPs

^bThe number average molecular weight of polypeptides was measured by gel permeation chromatography (GPC) equipped with refractive index detector and performed at 40 °C in DMF containing 0.4% LiBr with a flow rate of 1.0 ml min⁻¹

^cThe polydispersity indexes (PDI) were calculated based on universal calibration method using polystyrene standards

^dThe degrees of polymerization (DP) were obtained by the dividing of the Mw of polypeptide to Mw of peptide monomeric unit

^eThe cross-linking efficiency (CE%) was defined as molecular percentage that was used in gel network cross-linking

^fN/A means not available

^gThe gel with volume phase transition property