Table 2B.

Peptides Influencing Aβ Aggregation and Toxicity. β-sheet Breaking Peptides Based on the KLVFF Sequence

Name	Sequence	Description	D/L	Results	Reference
nn	KLVFF based, with chain of charged amino acids as disruption motif	β-sheet breaker	L	Enhance fibrillization of Aβ oligomers and therefore reduce Aβ toxicity. Effectiveness of inhibitor is dependent on its surface tension modifying properties	Ghanta et al., 1996; Pallitto et al., 1999; Lowe et al., 2001; Kim et al., 2004; Moss et al., 2003; Kim et al., 2003; Gibson et al., 2005 [69-75]
Aβ16-20e	KLVFF with ester sub-stitution	No hydrogen bond can be formed	L	Inhibit Aβ aggregation, disassembles fibrils. Expected to hydrolyze rapidly in vivo	Gordon et al., 2003 [77, 78]
AMY-1 AMY-2	KLVFF based	β-sheet breaker α,α-disubstituted amino acids	L	Inhibition of fibrillization, globular aggregates are formed	Etienne et al., 2006 [79]
P1, P2	KLVF-ΔA-I-ΔA and KF- ΔA- ΔA- ΔA-F	Disruption of aggregation by different local confirmation	L	Inhibit Aβ aggregation	Rangachari et al., 2009 [81]

D/L: describes peptide conformation. ΔAla: α, β-dehydroalanine. Aβ-derived peptide sequences are written in bold. Table