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Suckerin in squid sucker ring teeth is a block‐copolymer peptide comprised of two repeating modules—the alanine and histidine‐rich M1 and the glycine‐rich M2. Suckerin self‐assemblies display excellent thermo‐plasticity and pH‐responsive properties, along with the high biocompatibility, biodegradability, and sustainability. However, the self‐assembly mechanism and the detailed role of each module are still elusive, limiting the capability of applying and manipulating such biomaterials. Here, the self‐assembly dynamics of the two modules and two minimalist suckerin‐mimetic block‐copolymers, M1‐M2‐M1 and M2‐M1‐M2, in silico is investigated. The simulation results demonstrate that M2 has a stronger self‐association but weaker β‐sheet propensities than M1. The high self‐assembly propensity of M2 allows the minimalist block‐copolymer peptides to coalesce with microphase separation, enabling the formation of nanoconfined β‐sheets in the matrix formed by M1–M2 contacts. Since these glycine‐rich fragments with scatted hydrophobic and aromatic residues are building blocks of many other block‐copolymer peptides, the study suggests that these modules function as the “molecular glue” in addition to the flexible linker or spacer to drive the self‐assembly and microphase separation. The uncovered molecular insights may help understand the structure and function of suckerin and also aid in the design of functional block‐copolymer peptides for nanotechnology and biomedicine applications.