. 2020 Apr 7;118(10):2526–2536. doi: 10.1016/j.bpj.2020.03.023

Table 1.

Thermodynamics

		$Δ G_{c}^{o}$	$Δ G_{z i p}^{o}$
ILQINS	class 1 (P)	−28.1 (2)	−18.6 (1)
	class 5 (AP)	−28.9 (2)	−16.3 (2)

ΔΔG:	1–5:	+0.8	−2.3

IFQINS	class 1 (P)	−27.1 (1)	−20.5 (1)
	class 5 (AP)	−29.3 (2)	−16.4 (3)

ΔΔG:	1–5:	+2.2	−4.1

TFQINS	class 1 (P)	−26.1 (1)	−21.7 (2)
	class 5 (AP)	−29.5 (2)	−13.1 (2)

ΔΔG:	1–5:	+3.4	−8.6

Standard binding free energy gain to construct a buried interface in the direction of the β-sheet hydrogen-bonding axis ( $Δ G_{c}^{o}$ ) and the side-chain steric zipper interface ( $Δ G_{z i p}^{o}$ ). Units are kcal mol⁻¹ per peptide buried by the interface. AP is stronger (ΔΔG > 0) in terms of sheet elongation but is weaker (ΔΔG < 0) in zipper stability. Increasing in vitro amyloidogenicity for the sequence IL < IF < TF is matched by the strengthening of this trend in the ΔΔG-values.