Table 2.

Stimulus‐responsive peptide‐based self‐assemblies

Physiological stimulus	Peptide sequence	Features	Application	Ref.
	GALA (WEAALAEALAEALAEHLAEALAEALEALAA‐amide)	GALA interacts and destabilizes the lipid bilayers at acidic pH.	Drug, gene delivery, and cancer therapy	[156]
	pHMAPS (PpIX‐AEQNPIYWARYADWLFTTPLLLLDLALLVDADEGT)	Tumor acidic pH triggers a conformation switch of pHMAPS for inserting into tumor cell membranes.	Anti‐tumor growth and metastasis	[157]
pH	PA: C16‐KTTKS	As the pH decreases, the morphology of the material changes from tapes to twisted brils, to tapes, to micelles.		[61]
	PA: C16H6‐OEG	pH controls the reversible assembly and disassembly of nanofibers and spherical micelles.	Drug encapsulation and tumor accumulation	[62]
	PA: C16‐CCCCGGGS(P)‐RGD	At pH4, PA forms a long nanofibrous scaffold and disassembles when pH increases.		[52a]
	Cationic peptide: I6K5	The destruction of the nanoparticles occurred under acidic pH conditions.	Drug release	[63]
	PA: C16‐V3A3K3	Temperature affects the length of nanofibers.		[64]
Temperature	PA: C16‐VVVAAAKKK	The increase in temperature leads to an increase in the proportion of β‐sheet structures.		[65]
	PA: C16‐KKFFVLK	Temperature changes cause reversible thermal transitions between nanotubes and helical ribbons.		[66]
	Fmoc‐KCRGDK	The increase in temperature causes self‐assembled micelles to transform into assembled nanofibers.	Drug encapsulation for tumor immunotherapy	[158]
	KLVFFAK	Ionic strength tunes the size and yield of an amyloid‐like nanosheet.	Retroviral gene transduction	[68]
	FFD/GHK	Copper(II) ions promote the formation of nanofibrous hydrogels.		[69]
	GHK	GHK has a high affinity for copper(II) ions and spontaneously forms a tripeptide–copper complex (GHK‐Cu).	Wound healing	[71]
Ion	FF8 (KRRFFRRK)	Negatively charged lipid membranes induce self‐assembly of FF8.	Antibacterial	[72]
	Naproxen‐FF	Metal ions modulate the self‐assembly process and the mechanical properties of the hydrogel.		[114c]
	APAs: KSXEKS (X = variable amino acid residue)	The increase in ion concentration results in a transition from flat nanoribbons to twisting nanohelices.		[159]
	A series of seven‐residue peptides	Peptides can self‐assemble in the presence of transition‐metal ions to form catalytic amyloids.	Promoting hydrolytic and redox transformations	[160]
	Fmoc‐YP	ALP converts precursor to hydrogelator by dephosphorylation and then promotes self‐assembling.		[43]
	Nap‐D‐Phe‐D‐Phe‐D‐Tyr(H2PO3)		Cancer cell killing	[161]
	IR775‐Phe‐Phe‐Tyr(H2PO3)‐OH		Tumor PA imaging	[162]
	Nap‐FFGEY	Kinase and phosphatase regulate the formation/dissociation of self‐assembling nanostructures.		[78]
Enzyme	Fmoc‐dipeptide methyl esters	Subtilisin hydrolyzes methyl ester groups to promote self‐assembling.		[77]
	Nap‐phe‐phe‐NHCH2CH2OH	Esterase hydrolyzes ester bonds to promote the self‐assembly of the hydrogelator.	Cancer cell killing	[75]
	PhAc‐FFAGLDD	MMP‐9 digestion promotes the peptide structure from micellar aggregates to fibers.	Drug encapsulation, release, and cancer therapy	[76a,b]
	PA: C12‐GGRGDRPLGVRVVV	MMP‐2 digestion degrades peptide filaments and reassembles them into spherical micelles.	Drug release and tumor cell killing	[53]
	Olsa‐RVRR	Furin digestion and GSH reduction initiate a condensation reaction to promote the self‐assembly of nanostructures.	Tumor imaging and therapy	[163]