Reading the amino acid sequence of individual proteins with high precision and throughput holds promise to deliver the most detailed portrait of a biological cell. In the absence of natural mechanisms to copy, read, or transcribe protein sequences, abiological approaches to protein sequencing have taken a lead. One such approach is nanopore sequencing, where the amino acid sequence of a protein is read as the protein chain is moved through a nanopore reader. In contrast to DNA strand which carries a uniform negative charge regardless of its nucleotide sequence, capturing and keeping an unevenly charged peptide taut through the nanopore's constriction is a major challenge in nanopore sequencing of protein. Here, we use all-atom molecular dynamics simulations to explore the effective force experienced by heterogeneously charged peptides in a biological nanopore and the means to increase the force through protein engineering. We accomplish that by applying an external hydrostatic pressure that generates the water flow required to keep polypeptide chain under tension through the nanopore. The effective force on the peptide is measured by harmonically restraining one end of the peptide to a point in the pore vestibule. Our simulations have compared the effective force on the peptide applied by water flow in the most common biological nanopores used for sequencing: the truncated MspA, CsgG, alpha-hemolysin. Our results revealed the magnitude of the effective force applied to a peptide by a water flow, its dependence on the flow profile, and the amino acid composition of the peptide. The results of our simulations suggest a possibility of creating a high-performance engineered nanopore by increasing the electro-osmotic force introduced as a result of point mutations to the MspA structure.