Table 1.

The origins, amino acid sequences and molecular mechanisms of chondroinductive/chondroconductive peptides for cartilage tissue engineering.

Category	Sub-category	Name	Origin	Acid sequence	Molecular mechanisms	Refs.
Growth factor derived peptide	BMP signaling-derived peptide	CK2.1	The amino acid residues 466–469 of BMPR-IA	SYED	Inhibition of the CK2-BMPR-IA interaction led to the activation of the Smad signaling pathway	[99,104]
		BMP peptide	The amino acid residues 73–92 of the knuckle epitope of BMP-2	KIPKASSVPTELSAISTLYL	Activation of the BMP signaling pathway through BMP type I and type II receptors	[101,104,165]
		B2A	The amino acid residues 91–105 of BMP-2; heparin-binding motif	AISMLYLDENEKVVL; RKRKLERIAR	Activation of the ERK1/2, while inhibition p-Smad1/5/8 through binding to BMPR-IB and ActR-II	[38,109]
	TGF-β derived peptide	SPPEPS	The latency-associated protein region in TGF-β3	SPPEPS	Activation Insulin signaling pathways through GSK-3β	[110]
Extracellular matrix (ECM)-derived peptide	Cell-cell adhesion molecule-derived peptide	N-cadherin mimetic peptide	N-cadherin contains a His-Ala-Val (HAV) sequence	Ac-HAVDIGGGC; Ac-HAVDIGGKLDLKLDLKLDL; GGGHAVDI	Suppression of canonical Wnt signaling by increasing GSK-3β, then GSK-3β-mediated degradation of β-catenin/LEF-1/TCF complex	[41,53,118,121,122]
	ECM components-derived peptide	RGD	Integrin binding epitope in many ECM proteins	GGGGRGDY, GCGYGRGDSPG, GRGDSP, GGGGRGDSY	Activation of the Smad2 and ERK1/2 signaling pathways under the induction of TGF-β1	[42,[127], [128], [129], [130],132]
		Collagen mimetic peptide (CMP)	ECM	(P(hydroxyl)PG)x	Lacking	[137,138]
		GFOGER peptide	The amino acid residues 502–507 of the collagen I α1(I) chain	GFOGER	Lacking	[43,140,166]
		Glycopeptides	ECM	–	Lacking	[143,144]
		Link Protein N-terminal Peptide (LPP or link-N)	A cleaved N-terminal 16-amino peptide from link protein	DHLSDNYTLDHDRAIH	Activation of p-Smad1/5 through binding to BMPR-II and stimulating BMP-7	[55,153,154]