Underwater adhesives are critical for many applications, including marine coatings, sealants, and medical devices. Research on natural underwater adhesives has shown that L-3,4-dihydroxyphenylalanine (DOPA) and amyloid nanostructures are vital to their adhesive abilities. The fusion of DOPA-containing chains and amyloid-forming peptides creates a new space for designing underwater adhesives capable of multi-surface adhesion. One critical question for this design is the interplay between the DOPA and amyloid-forming peptide regions. Here we investigate the effect of the sequence pattern of DOPA-containing chains on the aggregation conformation of conjugates. Discontinuous molecular dynamics simulations were performed for fourteen DOPA-amyloid conjugates with different sequence patterns along the DOPA-containing portion. The amyloid-forming portion is represented by KLVFFAE from the Aβ 42 peptide. The structural properties of the DOPA-amyloid conjugates are characterised by the percentages of ordered secondary structures and residue-residue contact maps. The results showed that certain patterns of DOPA and glycine in the DOPA-containing tail allowed the KLVFFAE portions of the conjugates to form distinct ordered β-sheets, and the DOPA-containing portion and the KLVFFAE portion of the conjugates to remain separated both within the same chain and amongst different chains. Among the designs, the most promising sequences are KLVFFAE-G-YYGYYGYY (where Y represents DOPA) and KLVFFAE-G-YYYYGGGG.