Ancient peptides
are remnants of early biochemistry that continue
to play pivotal roles in current proteins. They are simple molecules
yet complex enough to exhibit independent functions, being products
of an evolved biochemistry at the interface of life and nonlife. Their
adsorption to minerals may contribute to their stabilization and preservation
over time. To investigate the feasibility of conserved peptide sequences
and structures as target biomarkers for the search for life on Mars
or other planetary bodies, we conducted a bioinformatics selection
of well-conserved ancient peptides and produced polyclonal antibodies
for their detection using fluorescence microarray immunoassays. Additionally,
we explored how adsorbing peptides to Mars-representative minerals
to form organomineral complexes could affect their immunological detection.
The results demonstrated that the selected peptides exhibited autonomous
folding, with some of them regaining their structure, even after denaturation.
Furthermore, their cognate antibodies detected their conformational
features regardless of amino acid sequences, thereby broadening the
spectrum of target peptide sequences. While certain antibodies displayed
unspecific binding to bare minerals, we validated that peptide–mineral
complexes can be detected using sandwich immunoassays, as confirmed
through desorption and competitive assays. Consequently, we conclude
that the diversity of peptide sequences and structures suitable for
use as target biomarkers in astrobiology can be constrained to a few
well conserved sets, and they can be detected even if they are adsorbed
in organomineral complexes.